{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T09:17:27Z","timestamp":1788427047032,"version":"build-2803163510"},"reference-count":81,"publisher":"Portland Press Ltd.","issue":"10","license":[{"start":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T00:00:00Z","timestamp":1787184000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/2.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health","doi-asserted-by":"publisher","award":["R21 AI124681"],"award-info":[{"award-number":["R21 AI124681"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health","doi-asserted-by":"publisher","award":["P01 HL15133"],"award-info":[{"award-number":["P01 HL15133"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2026,10,7]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Glycosaminoglycans (GAGs) play diverse and fundamental roles in physiology by regulating the function of large classes of proteins. Despite their importance, knowledge of how GAGs are organized in protein-bound complexes remains limited. This can be attributed to the linear structure, conformational flexibility, and high negative charge of GAGs, all of which disfavor structure determination by crystallography or NMR spectroscopy. A hybrid approach based on GAG-binding-induced changes in NMR protein chemical shifts, computational docking, and molecular dynamics simulations has proven to be valuable in providing structural models. However, these approaches can identify multiple plausible GAG geometries, making it difficult to determine whether the observed geometries reflect intrinsic plasticity or limitations of the NMR data and docking methods. In the case of chemokine CXCL8, two GAG-binding modes have been proposed, one within a monomer and the other across the dimer interface. Here, we determined low-resolution solution structures of heparin and chondroitin sulfate octasaccharides bound to the CXCL8 dimer using small-angle X-ray scattering (SAXS). SAXS analyses show that both heparin and chondroitin sulfate bind to a surface within a monomer and are incompatible with binding across the dimer. NMR paramagnetic relaxation enhancement measurements for heparin-bound CXCL8 dimer and monomer complexes show that heparin engages a similar surface within the monomer in both complexes, consistent with the SAXS models. Together, these studies establish how GAGs are organized in the CXCL8-bound complex and highlight the value of complementary low-resolution structural methods for characterizing GAG\u2013protein complexes.<\/jats:p>","DOI":"10.1042\/bcj20260348","type":"journal-article","created":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T05:04:59Z","timestamp":1787202299000},"page":"1861-1876","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Solution structures of glycosaminoglycan-bound CXCL8 complexes determined by small-angle X-ray scattering (SAXS)"],"prefix":"10.1042","volume":"483","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1057-4203","authenticated-orcid":false,"given":"Mark\u00a0A.","family":"White","sequence":"first","affiliation":[{"name":"1Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, U.S.A."},{"name":"2Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bryon\u00a0P.","family":"Mahler","sequence":"additional","affiliation":[{"name":"1Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, U.S.A."},{"name":"2Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Prem\u00a0Raj\u00a0B.","family":"Joseph","sequence":"additional","affiliation":[{"name":"1Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, U.S.A."},{"name":"2Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Balaji","family":"Nagarajan","sequence":"additional","affiliation":[{"name":"3Department of Medicinal Chemistry and Center for Drug Discovery, Virginia Commonwealth University, Richmond, Virginia 23219, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xu","family":"Wang","sequence":"additional","affiliation":[{"name":"4School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1976-6597","authenticated-orcid":false,"given":"Umesh\u00a0R.","family":"Desai","sequence":"additional","affiliation":[{"name":"3Department of Medicinal Chemistry and Center for Drug Discovery, Virginia Commonwealth University, Richmond, Virginia 23219, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0077-700X","authenticated-orcid":false,"given":"Krishna","family":"Rajarathnam","sequence":"additional","affiliation":[{"name":"1Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, U.S.A."},{"name":"2Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2026,9,3]]},"reference":[{"key":"2026090304464400900_B1","doi-asserted-by":"publisher","first-page":"150","DOI":"10.4161\/cib.4.2.14547","article-title":"Evolution of glycosaminoglycans: comparative biochemical study","volume":"4","author":"Yamada","year":"2011","journal-title":"Commun. 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