1b9p: Difference between revisions
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==NMR STRUCTURE OF HEPARIN BINDING SITE OF NON COLLAGENOUS DOMAIN I (NC1) OF COLLAGEN FACIT XIV== | ==NMR STRUCTURE OF HEPARIN BINDING SITE OF NON COLLAGENOUS DOMAIN I (NC1) OF COLLAGEN FACIT XIV== | ||
<StructureSection load='1b9p' size='340' side='right' caption='[[1b9p | <StructureSection load='1b9p' size='340' side='right'caption='[[1b9p]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1b9p]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9P OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[1b9p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B9P FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b9p OCA], [https://pdbe.org/1b9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b9p RCSB], [https://www.ebi.ac.uk/pdbsum/1b9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b9p ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/COEA1_CHICK COEA1_CHICK] An adhesive role by integrating collagen bundles. It is probably associated with the surface of interstitial collagen fibrils via COL1. The COL2 domain may then serve as a rigid arm which sticks out from the fibril and protrudes the large N-terminal globular domain into the extracellular space, where it might interact with other matrix molecules or cell surface receptors. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1b9p" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Collagen|Collagen]] | *[[Collagen 3D structures|Collagen 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Deleage G]] | ||
[[Category: | [[Category: Montserret R]] | ||
[[Category: | [[Category: Penin F]] | ||