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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN] Type I collagen is a member of group I collagen (fibrillar forming collagen). | | [https://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN] Type I collagen is a member of group I collagen (fibrillar forming collagen). |
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| == Publication Abstract from PubMed ==
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| The proteolysis of collagen triple-helical structure (collagenolysis) is a poorly understood yet critical physiological process. Presently, matrix metalloproteinase 1 (MMP-1) and collagen triple-helical peptide models have been utilized to characterize the events and calculate the energetics of collagenolysis via NMR spectroscopic analysis of 12 enzyme-substrate complexes. The triple-helix is bound initially by the MMP-1 hemopexin-like (HPX) domain via a four amino acid stretch (analogous to type I collagen residues 782-785). The triple-helix is then presented to the MMP-1 catalytic (CAT) domain in a distinct orientation. The HPX and CAT domains are rotated with respect to one another compared with the X-ray "closed" conformation of MMP-1. Back-rotation of the CAT and HPX domains to the X-ray closed conformation releases one chain out of the triple-helix, and this chain is properly positioned in the CAT domain active site for subsequent hydrolysis. The aforementioned steps provide a detailed, experimentally derived, and energetically favorable collagenolytic mechanism, as well as significant insight into the roles of distinct domains in extracellular protease function.
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| Structural basis for matrix metalloproteinase 1-catalyzed collagenolysis.,Bertini I, Fragai M, Luchinat C, Melikian M, Toccafondi M, Lauer JL, Fields GB J Am Chem Soc. 2012 Feb 1;134(4):2100-10. Epub 2012 Jan 19. PMID:22239621<ref>PMID:22239621</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 2llp" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
