3n3f: Difference between revisions
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<StructureSection load='3n3f' size='340' side='right'caption='[[3n3f]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3n3f' size='340' side='right'caption='[[3n3f]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3n3f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3n3f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N3F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N3F FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.005Å</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=3n3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n3f OCA], [https://pdbe.org/3n3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n3f RCSB], [https://www.ebi.ac.uk/pdbsum/3n3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n3f ProSAT]</span></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=3n3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n3f OCA], [https://pdbe.org/3n3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n3f RCSB], [https://www.ebi.ac.uk/pdbsum/3n3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n3f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/COFA1_HUMAN COFA1_HUMAN] Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle.<ref>PMID:10049780</ref> Restin potently inhibits angiogenesis. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Wirz | [[Category: Wirz JA]] | ||
Latest revision as of 12:08, 6 September 2023
Crystal Structure of the Human Collagen XV Trimerization Domain: A Potent Trimerizing Unit Common to Multiplexin CollagensCrystal Structure of the Human Collagen XV Trimerization Domain: A Potent Trimerizing Unit Common to Multiplexin Collagens
Structural highlights
FunctionCOFA1_HUMAN Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle.[1] Restin potently inhibits angiogenesis. Publication Abstract from PubMedCorrect folding of the collagen triple helix requires a self-association step which selects and binds alpha-chains into trimers. Here we report the crystal structure of the trimerization domain of human type XV collagen. The trimerization domain of type XV collagen contains three monomers each composed of four beta-sheets and an alpha-helix. The hydrophobic core of the trimer is devoid of solvent molecules and is shaped by beta-sheet planes from each monomer. The trimerization domain is extremely stable and forms at picomolar concentrations. It is found that the trimerization domain of type XV collagen is structurally similar to that of type XVIII, despite only 32% sequence identity. High structural conservation indicates that the multiplexin trimerization domain represents a three dimensional fold that allows for sequence variability while retaining structural integrity necessary for tight and efficient trimerization. Crystal structure of the human collagen XV trimerization domain: A potent trimerizing unit common to multiplexin collagens.,Wirz JA, Boudko SP, Lerch TF, Chapman MS, Bachinger HP Matrix Biol. 2010 Oct 12. PMID:20932905[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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