{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T11:46:49Z","timestamp":1778932009801,"version":"3.51.4"},"reference-count":30,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2020,6,11]],"date-time":"2020-06-11T00:00:00Z","timestamp":1591833600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100012226","name":"Fundamental Research Funds for the Central Universities","doi-asserted-by":"publisher","award":["2452019074"],"award-info":[{"award-number":["2452019074"]}],"id":[{"id":"10.13039\/501100012226","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Development and Research Center of Sichuan Cuisine, Sichuan Provincial Department of Education","award":["CC18Z16"],"award-info":[{"award-number":["CC18Z16"]}]},{"name":"U.S. Department of Energy (DOE) Office of Science User Facility","award":["DE-AC02-06CH11357"],"award-info":[{"award-number":["DE-AC02-06CH11357"]}]},{"name":"National Institute of General Medical Sciences of the National Institutes of Health","award":["9 P41 GM103622"],"award-info":[{"award-number":["9 P41 GM103622"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Collagen type I is a major constituent of animal bodies. It is found in large quantities in tendon, bone, skin, cartilage, blood vessels, bronchi, and the lung interstitium. It is also produced and accumulates in large amounts in response to certain inflammations such as lung fibrosis. Our understanding of the molecular organization of fibrillar collagen and cellular interaction motifs, such as those involved with immune-associated molecules, continues to be refined. In this study, antibodies raised against type I collagen were used to label intact D-periodic type I collagen fibrils and observed with atomic force microscopy (AFM), and X-ray diffraction (XRD) and immunolabeling positions were observed with both methods. The antibodies bind close to the C-terminal telopeptide which verifies the location and accessibility of both the major histocompatibility complex (MHC) class I (MHCI) binding domain and C-terminal telopeptide on the outside of the collagen fibril. The close proximity of the C-telopeptide and the MHC1 domain of type I collagen to fibronectin, discoidin domain receptor (DDR), and collagenase cleavage domains likely facilitate the interaction of ligands and receptors related to cellular immunity and the collagen-based Extracellular Matrix.<\/jats:p>","DOI":"10.3390\/ijms21114166","type":"journal-article","created":{"date-parts":[[2020,6,15]],"date-time":"2020-06-15T03:17:32Z","timestamp":1592191052000},"page":"4166","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Ultrastructural Location and Interactions of the Immunoglobulin Receptor Binding Sequence within Fibrillar Type I Collagen"],"prefix":"10.3390","volume":"21","author":[{"given":"Jie","family":"Zhu","sequence":"first","affiliation":[{"name":"Institute of Biophysics, College of science, Northwest A&amp;F University, Yangling 712100, China"},{"name":"Department of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA"},{"name":"Pritzker Institute of Biomedical Science and Engineering, Illinois Institute of Technology, Chicago, IL 60616, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9477-9171","authenticated-orcid":false,"given":"Rama","family":"Madhurapantula","sequence":"additional","affiliation":[{"name":"Department of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA"},{"name":"Pritzker Institute of Biomedical Science and Engineering, Illinois Institute of Technology, Chicago, IL 60616, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aruna","family":"Kalyanasundaram","sequence":"additional","affiliation":[{"name":"Department of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tanya","family":"Sabharwal","sequence":"additional","affiliation":[{"name":"Department of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Olga","family":"Antipova","sequence":"additional","affiliation":[{"name":"Department of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA"},{"name":"X-ray Science Division, Argonne National Laboratory, Lemont, IL 60439, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sandra","family":"Bishnoi","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Illinois Institute of Technology, Chicago, IL 60616, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1050-9391","authenticated-orcid":false,"given":"Joseph","family":"Orgel","sequence":"additional","affiliation":[{"name":"Department of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA"},{"name":"Pritzker Institute of Biomedical Science and Engineering, Illinois Institute of Technology, Chicago, IL 60616, USA"},{"name":"Department of Biomedical Engineering, Illinois Institute of Technology, Chicago, IL 60616, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2020,6,11]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2","DOI":"10.3109\/03008207.2010.511353","article-title":"Molecular and structural mapping of collagen fibril interactions","volume":"52","author":"Orgel","year":"2011","journal-title":"Connect. Tissue Res."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"9001","DOI":"10.1073\/pnas.0502718103","article-title":"Microfibrillar structure of type I collagen in situ","volume":"103","author":"Orgel","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S0969-2126(00)00089-7","article-title":"The in situ conformation and axial location of the intermolecular cross-linked non-helical telopeptides of type I collagen","volume":"8","author":"Orgel","year":"2000","journal-title":"Structure"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1182\/blood-2006-01-010215","article-title":"Structural basis for platelet collagen responses by the immune-type receptor glycoprotein VI","volume":"108","author":"Horii","year":"2006","journal-title":"Blood"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"3592","DOI":"10.1091\/mbc.e02-12-0814","article-title":"Identification and characterization of the endocytic transmembrane glycoprotein Endo180 as a novel collagen receptor","volume":"14","author":"Wienke","year":"2003","journal-title":"Mol. Biol. Cell"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1038","DOI":"10.1073\/pnas.1522572113","article-title":"Structural basis of collagen recognition by human osteoclast-associated receptor and design of osteoclastogenesis inhibitors","volume":"113","author":"Haywood","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"118478","DOI":"10.1016\/j.bbamcr.2019.04.008","article-title":"A structural prospective for collagen receptors such as DDR and their binding of the collagen fibril","volume":"1866","author":"Orgel","year":"2019","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"21187","DOI":"10.1074\/jbc.M709319200","article-title":"Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates","volume":"283","author":"Sweeney","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2824","DOI":"10.1073\/pnas.0710588105","article-title":"Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis","volume":"105","author":"Perumal","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"18","DOI":"10.3109\/03008207.2010.511354","article-title":"Collagen fibril surface displays a constellation of sites capable of promoting fibril assembly, stability, and hemostasis","volume":"52","author":"Orgel","year":"2011","journal-title":"Connect.proline Tissue Res."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"30000","DOI":"10.1074\/jbc.M112.359125","article-title":"Constitutive dimerization of glycoprotein VI (GPVI) in resting platelets is essential for binding to collagen and activation in flowing blood","volume":"287","author":"Jung","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"46197","DOI":"10.1074\/jbc.M204029200","article-title":"Analysis of the interaction of platelet collagen receptor glycoprotein VI (GPVI) with collagen. A dimeric form of GPVI, but not the monomeric form, shows affinity to fibrous collagen","volume":"277","author":"Miura","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1111\/jth.13613","article-title":"Clustering of glycoprotein VI (GPVI) dimers upon adhesion to collagen as a mechanism to regulate GPVI signaling in platelets","volume":"15","author":"Poulter","year":"2017","journal-title":"J. Thromb. Haemost."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1016\/S0969-2126(01)00669-4","article-title":"The in situ supermolecular structure of type I collagen","volume":"9","author":"Orgel","year":"2001","journal-title":"Structure"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"12","DOI":"10.3389\/fphy.2017.00012","article-title":"Collagen type I as a ligand for receptor-mediated signaling","volume":"5","author":"Wang","year":"2017","journal-title":"Front. Phys."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"181902","DOI":"10.1063\/1.2367660","article-title":"Determination of the elastic modulus of native collagen fibrils via radial indentation","volume":"89","author":"Heim","year":"2006","journal-title":"Appl. Phys. Lett."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.bbrc.2006.12.114","article-title":"Structural investigations on native collagen type I fibrils using AFM","volume":"354","author":"Strasser","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"233902","DOI":"10.1063\/1.2937001","article-title":"Effects of hydration on the mechanical response of individual collagen fibrils","volume":"92","author":"Grant","year":"2008","journal-title":"Appl. Phys. Lett."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"7087","DOI":"10.1074\/jbc.M109.060400","article-title":"In situ D-periodic molecular structure of type II collagen","volume":"285","author":"Antipova","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Orgel, J.P., and Irving, T.C. (2014). Advances in Fiber Diffraction of Macromolecular Assembles. Encyclopedia of Analytical Chemistry, American Cancer Society.","DOI":"10.1002\/9780470027318.a9420"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/0022-2836(79)90507-2","article-title":"Chain conformation in the collagen molecule","volume":"129","author":"Fraser","year":"1979","journal-title":"J. Mol. Biol."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Orgel, J.P.R.O., Persikov, A.V., and Antipova, O. (2014). Variation in the helical structure of native collagen. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0089519"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1042\/BJ20151169","article-title":"Collagen structure: New tricks from a very old dog","volume":"473","author":"Bella","year":"2016","journal-title":"Biochem. J."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1016\/j.micron.2006.07.026","article-title":"Influence of saline and pH on collagen type I fibrillogenesis in vitro: Fibril polymorphism and colloidal gold labelling","volume":"38","author":"Harris","year":"2007","journal-title":"Micron"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"4053","DOI":"10.1021\/ac103195e","article-title":"SERS biodetection using gold\u2013silica nanoshells and nitrocellulose membranes","volume":"83","author":"Bishnoi","year":"2011","journal-title":"Anal. Chem."},{"key":"ref_26","first-page":"172","article-title":"Study on the original height and compression elasticity of the DNA strands with atomic force microscopy","volume":"25","author":"Zhu","year":"2008","journal-title":"Chin. J. Appl. Mech."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Orgel, J.P.R.O., Eid, A., Antipova, O., Bella, J., and Scott, J.E. (2009). Decorin core protein (decoron) shape complements collagen fibril surface structure and mediates its binding. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0007028"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"D520","DOI":"10.1093\/nar\/gky949","article-title":"Protein Data Bank: The single global archive for 3D macromolecular structure data","volume":"47","author":"Burley","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Hoop, C., Zhu, J., Nunes, A., Case, D., and Baum, J. (2017). Revealing Accessibility of Cryptic Protein Binding Sites within the Functional Collagen Fibril. Biomolecules, 7.","DOI":"10.3390\/biom7040076"},{"key":"ref_30","first-page":"406","article-title":"Collagen fragments modulate innate immunity","volume":"232","author":"Thomas","year":"2007","journal-title":"Exp. Biol. Med."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/11\/4166\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T09:37:45Z","timestamp":1760175465000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/11\/4166"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,6,11]]},"references-count":30,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2020,6]]}},"alternative-id":["ijms21114166"],"URL":"https:\/\/doi.org\/10.3390\/ijms21114166","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,6,11]]}}}