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1rm8
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1rm8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RM8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RM8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1rm8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RM8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RM8 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BAT:4-(N-HYDROXYAMINO)-2R-ISOBUTYL-2S-(2-THIENYLTHIOMETHYL)SUCCINYL-L-PHENYLALANINE-N-METHYLAMIDE'>BAT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BAT:4-(N-HYDROXYAMINO)-2R-ISOBUTYL-2S-(2-THIENYLTHIOMETHYL)SUCCINYL-L-PHENYLALANINE-N-METHYLAMIDE'>BAT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bqq|1bqq]], [[1jk3|1jk3]], [[1mmb|1mmb]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bqq|1bqq]], [[1jk3|1jk3]], [[1mmb|1mmb]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rm8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rm8 RCSB], [http://www.ebi.ac.uk/pdbsum/1rm8 PDBsum]</span></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=1rm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rm8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rm8 RCSB], [http://www.ebi.ac.uk/pdbsum/1rm8 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MMP16_HUMAN MMP16_HUMAN]] Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Bode, W | + | [[Category: Bode, W]] |
| - | [[Category: Braun, M | + | [[Category: Braun, M]] |
| - | [[Category: Foidart, J M | + | [[Category: Foidart, J M]] |
| - | [[Category: Frankenne, F | + | [[Category: Frankenne, F]] |
| - | [[Category: Lang, R | + | [[Category: Lang, R]] |
| - | [[Category: Maskos, K | + | [[Category: Maskos, K]] |
[[Category: Noel, A]] | [[Category: Noel, A]] | ||
| - | [[Category: Sounni, N E | + | [[Category: Sounni, N E]] |
[[Category: Batimastat]] | [[Category: Batimastat]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 19:36, 24 December 2014
Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features
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