{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T04:06:30Z","timestamp":1792037190397,"version":"4.4.0"},"reference-count":35,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"5182","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[1994,10,7]]},"abstract":"<jats:p>\n            The structure of a protein triple helix has been determined at 1.9 angstrom resolution by x-ray crystallographic studies of a collagen-like peptide containing a single substitution of the consensus sequence. This peptide adopts a triple-helical structure that confirms the basic features determined from fiber diffraction studies on collagen: supercoiling of polyproline II helices and interchain hydrogen bonding that follows the model II of Rich and Crick. In addition, the structure provides new information concerning the nature of this protein fold. Each triple helix is surrounded by a cylinder of hydration, with an extensive hydrogen bonding network between water molecules and peptide acceptor groups. Hydroxyproline residues have a critical role in this water network. The interaxial spacing of triple helices in the crystal is similar to that in collagen fibrils, and the water networks linking adjacent triple helices in the crystal structure are likely to be present in connective tissues. The breaking of the repeating (X-Y-Gly)\n            <jats:sub>\n              <jats:italic>n<\/jats:italic>\n            <\/jats:sub>\n            pattern by a Gly\u2192Ala substitution results in a subtle alteration of the conformation, with a local untwisting of the triple helix. At the substitution site, direct interchain hydrogen bonds are replaced with interstitial water bridges between the peptide groups. Similar conformational changes may occur in Gly\u2192X mutated collagens responsible for the diseases osteogenesis imperfecta, chondrodysplasias, and Ehlers-Danlos syndrome IV.\n          <\/jats:p>","DOI":"10.1126\/science.7695699","type":"journal-article","created":{"date-parts":[[2006,10,6]],"date-time":"2006-10-06T00:01:25Z","timestamp":1160092885000},"page":"75-81","source":"Crossref","is-referenced-by-count":987,"title":["Crystal and Molecular Structure of a Collagen-Like Peptide at 1.9 \u00c5 Resolution"],"prefix":"10.1126","volume":"266","author":[{"given":"Jordi","family":"Bella","sequence":"first","affiliation":[{"name":"Department of Chemistry, Rutgers University, New Brunswick, NJ 08855."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark","family":"Eaton","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Rutgers University, New Brunswick, NJ 08855."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Barbara","family":"Brodsky","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Helen M.","family":"Berman","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Rutgers University, New Brunswick, NJ 08855."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","reference":[{"key":"e_1_2_1_1_1","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1021\/ar00089a001","volume":"16","year":"1983","unstructured":"ALLEN, F.H., SYSTEMATIC ANALYSIS OF STRUCTURAL DATA AS A RESEARCH TECHNIQUE IN ORGANIC-CHEMISTRY, ACCOUNTS OF CHEMICAL RESEARCH 16: 146 (1983).","journal-title":"ACCOUNTS OF CHEMICAL RESEARCH"},{"key":"e_1_2_1_2_1","unstructured":"BELLA J unpublished data."},{"key":"e_1_2_1_3_1","doi-asserted-by":"crossref","first-page":"5759","DOI":"10.1016\/S0021-9258(18)62717-6","volume":"245","year":"1970","unstructured":"BERG, R.A., TITRATION AND MELTING CURVES OF COLLAGEN-LIKE TRIPLE HELICES FORMED FROM(PRO-PRO-GLY)10 IN AQUEOUS SOLUTION, JOURNAL OF BIOLOGICAL CHEMISTRY 245: 5759 (1970).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"key":"e_1_2_1_4_1","doi-asserted-by":"crossref","first-page":"22522","DOI":"10.1016\/S0021-9258(18)41703-6","volume":"267","year":"1992","unstructured":"BOGAERT, R, AN AMINO-ACID SUBSTITUTION (GLY853 -] GLU) IN THE COLLAGEN ALPHA-1(II) CHAIN PRODUCES HYPOCHONDROGENESIS, JOURNAL OF BIOLOGICAL CHEMISTRY 267: 22522 (1992).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"key":"e_1_2_1_5_1","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1042\/bj1590279","volume":"159","year":"1976","unstructured":"BRODSKYDOYLE, B, CIRCULAR-DICHROISM AND ELECTRON-MICROSCOPY STUDIES OF HUMAN SUBCOMPONENT C1Q BEFORE AND AFTER LIMITED PROTEOLYSIS BY PEPSIN, BIOCHEMICAL JOURNAL 159: 279 (1976).","journal-title":"BIOCHEMICAL JOURNAL"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.235.4787.458"},{"key":"e_1_2_1_7_1","unstructured":"Brunger A. 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