966c

<StructureSection load='966c' size='340' side='right' caption='[[966c]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[966c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=966C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=966C FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=RS2:N-HYDROXY-2-[4-(4-PHENOXY-BENZENESULFONYL)-TETRAHYDRO-PYRAN-4-YL]-ACETAMIDE'>RS2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=966c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=966c OCA], [http://pdbe.org/966c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=966c RCSB], [http://www.ebi.ac.uk/pdbsum/966c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=966c ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MMP1_HUMAN MMP1_HUMAN]] Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.<ref>PMID:1645757</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The X-ray crystal structures of the catalytic domain of human collagenase-3 (MMP-13) and collagenase-1 (MMP-1) with bound inhibitors provides a basis for understanding the selectivity profile of a novel series of matrix metalloprotease (MMP) inhibitors. Differences in the relative size and shape of the MMP S1' pockets suggest that this pocket is a critical determinant of MMP inhibitor selectivity. The collagenase-3 S1' pocket is long and open, easily accommodating large P1' groups, such as diphenylether. In contrast, the collagenase-1 S1' pocket must undergo a conformational change to accommodate comparable P1' groups. The selectivity of the diphenylether series of inhibitors for collagenase-3 is largely determined by their affinity for the preformed S1' pocket of collagenase-3, as compared to the induced fit in collagenase-1.

Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors.,Lovejoy B, Welch AR, Carr S, Luong C, Broka C, Hendricks RT, Campbell JA, Walker KA, Martin R, Van Wart H, Browner MF Nat Struct Biol. 1999 Mar;6(3):217-21. PMID:10074939<ref>PMID:10074939</ref>

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

</div>

<div class="pdbe-citations 966c" style="background-color:#fffaf0;"></div>

*[[Matrix metalloproteinase|Matrix metalloproteinase]]

[[Category: Human]]

[[Category: Broka, C]]

[[Category: Browner, M F]]

[[Category: Campbell, J]]

[[Category: Carr, S]]

[[Category: Hendricks, R T]]

[[Category: Lovejoy, B]]

[[Category: Luong, C]]

[[Category: Martin, R]]

[[Category: Walker, K]]

[[Category: Wart, H Van]]

[[Category: Welch, A]]

[[Category: Matrix metalloprotease]]