3hr2

<table><tr><td colspan='2'>[[3hr2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1y0f 1y0f]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HR2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3HR2 FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=LYZ:5-HYDROXYLYSINE'>LYZ</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y0f|1y0f]], [[3hqv|3hqv]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3hr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hr2 OCA], [http://pdbe.org/3hr2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hr2 RCSB], [http://www.ebi.ac.uk/pdbsum/3hr2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hr2 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CO1A1_RAT CO1A1_RAT]] Type I collagen is a member of group I collagen (fibrillar forming collagen). [[http://www.uniprot.org/uniprot/CO1A2_RAT CO1A2_RAT]] Type I collagen is a member of group I collagen (fibrillar forming collagen).

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== Publication Abstract from PubMed ==

The fibrous collagens are ubiquitous in animals and form the structural basis of all mammalian connective tissues, including those of the heart, vasculature, skin, cornea, bones, and tendons. However, in comparison with what is known of their production, turnover and physiological structure, very little is understood regarding the three-dimensional arrangement of collagen molecules in naturally occurring fibrils. This knowledge may provide insight into key biological processes such as fibrillo-genesis and tissue remodeling and into diseases such as heart disease and cancer. Here we present a crystallographic determination of the collagen type I supermolecular structure, where the molecular conformation of each collagen segment found within the naturally occurring crystallographic unit cell has been defined (P1, a approximately 40.0 A, b approximately 27.0 A, c approximately 678 A, alpha approximately 89.2 degrees , beta approximately 94.6 degrees , gamma approximately 105.6 degrees ; reflections: 414, overlapping, 232, and nonoverlapping, 182; resolution, 5.16 A axial and 11.1 A equatorial). This structure shows that the molecular packing topology of the collagen molecule is such that packing neighbors are arranged to form a supertwisted (discontinuous) right-handed microfibril that interdigitates with neighboring microfibrils. This interdigitation establishes the crystallographic superlattice, which is formed of quasihexagonally packed collagen molecules. In addition, the molecular packing structure of collagen shown here provides information concerning the potential modes of action of two prominent molecules involved in human health and disease: decorin and the Matrix Metallo-Proteinase (MMP) collagenase.

Microfibrillar structure of type I collagen in situ.,Orgel JP, Irving TC, Miller A, Wess TJ Proc Natl Acad Sci U S A. 2006 Jun 13;103(24):9001-5. Epub 2006 Jun 2. PMID:16751282<ref>PMID:16751282</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Orgel, J P]]

[[Category: Triple-helical]]