830c

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{{Seed}}
 
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[[Image:830c.png|left|200px]]
 
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==COLLAGENASE-3 (MMP-13) COMPLEXED TO A SULPHONE-BASED HYDROXAMIC ACID==
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The line below this paragraph, containing "STRUCTURE_830c", creates the "Structure Box" on the page.
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<StructureSection load='830c' size='340' side='right'caption='[[830c]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[830c]] 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=830C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=830C FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=RS1:4-[4-(4-CHLORO-PHENOXY)-BENZENESULFONYLMETHYL]-TETRAHYDRO-PYRAN-4-CARBOXYLIC+ACID+HYDROXYAMIDE'>RS1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_830c| PDB=830c | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=830c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=830c OCA], [https://pdbe.org/830c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=830c RCSB], [https://www.ebi.ac.uk/pdbsum/830c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=830c ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/MMP13_HUMAN MMP13_HUMAN] Defects in MMP13 are the cause of spondyloepimetaphyseal dysplasia Missouri type (SEMD-MO) [MIM:[https://omim.org/entry/602111 602111]. A bone disease characterized by moderate to severe metaphyseal changes, mild epiphyseal involvement, rhizomelic shortening of the lower limbs with bowing of the femora and/or tibiae, coxa vara, genu varum and pear-shaped vertebrae in childhood. Epimetaphyseal changes improve with age.<ref>PMID:16167086</ref> Defects in MMP13 are the cause of metaphyseal anadysplasia type 1 (MANDP1) [MIM:[https://omim.org/entry/602111 602111]. Metaphyseal anadysplasia consists of an abnormal bone development characterized by severe skeletal changes that, in contrast with the progressive course of most other skeletal dysplasias, resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.<ref>PMID:19615667</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/MMP13_HUMAN MMP13_HUMAN] Degrades collagen type I. Does not act on gelatin or casein. Could have a role in tumoral process.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/30/830c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=830c ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===COLLAGENASE-3 (MMP-13) COMPLEXED TO A SULPHONE-BASED HYDROXAMIC ACID===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 830c" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10074939}}, adds the Publication Abstract to the page
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*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10074939 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10074939}}
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__TOC__
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</StructureSection>
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==About this Structure==
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830C is a [[Single protein]] structure of 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=830C OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10074939 10074939]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Broka, C.]]
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[[Category: Broka C]]
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[[Category: Browner, M F.]]
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[[Category: Browner MF]]
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[[Category: Campbell, J.]]
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[[Category: Campbell J]]
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[[Category: Carr, S.]]
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[[Category: Carr S]]
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[[Category: Hendricks, R T.]]
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[[Category: Hendricks RT]]
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[[Category: Lovejoy, B.]]
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[[Category: Lovejoy B]]
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[[Category: Luong, C.]]
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[[Category: Luong C]]
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[[Category: Martin, R.]]
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[[Category: Martin R]]
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[[Category: Walker, K.]]
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[[Category: Van Wart H]]
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[[Category: Wart, H Van.]]
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[[Category: Walker K]]
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[[Category: Welch, A.]]
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[[Category: Welch A]]
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[[Category: Matrix metalloprotease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Jul 11 12:55:28 2008''
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Current revision

COLLAGENASE-3 (MMP-13) COMPLEXED TO A SULPHONE-BASED HYDROXAMIC ACID

PDB ID 830c

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