1hov

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[[Image:1hov.gif|left|200px]]<br /><applet load="1hov" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hov.gif|left|200px]]
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caption="1hov" />
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'''SOLUTION STRUCTURE OF A CATALYTIC DOMAIN OF MMP-2 COMPLEXED WITH SC-74020'''<br />
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{{Structure
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|PDB= 1hov |SIZE=350|CAPTION= <scene name='initialview01'>1hov</scene>
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=I52:N-{4-[(1-HYDROXYCARBAMOYL-2-METHYL-PROPYL)-(2-MORPHOLIN-4-YL-ETHYL)-SULFAMOYL]-4-PENTYL-BENZAMIDE'>I52</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Gelatinase_A Gelatinase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.24 3.4.24.24]
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|GENE=
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}}
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'''SOLUTION STRUCTURE OF A CATALYTIC DOMAIN OF MMP-2 COMPLEXED WITH SC-74020'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1HOV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=I52:'>I52</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Gelatinase_A Gelatinase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.24 3.4.24.24] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HOV OCA].
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1HOV 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=1HOV OCA].
==Reference==
==Reference==
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Solution structure and backbone dynamics of the catalytic domain of matrix metalloproteinase-2 complexed with a hydroxamic acid inhibitor., Feng Y, Likos JJ, Zhu L, Woodward H, Munie G, McDonald JJ, Stevens AM, Howard CP, De Crescenzo GA, Welsch D, Shieh HS, Stallings WC, Biochim Biophys Acta. 2002 Jul 29;1598(1-2):10-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12147339 12147339]
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Solution structure and backbone dynamics of the catalytic domain of matrix metalloproteinase-2 complexed with a hydroxamic acid inhibitor., Feng Y, Likos JJ, Zhu L, Woodward H, Munie G, McDonald JJ, Stevens AM, Howard CP, De Crescenzo GA, Welsch D, Shieh HS, Stallings WC, Biochim Biophys Acta. 2002 Jul 29;1598(1-2):10-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12147339 12147339]
[[Category: Gelatinase A]]
[[Category: Gelatinase A]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: enzyme-inhibitor complex]]
[[Category: enzyme-inhibitor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:39:45 2008''

Revision as of 09:39, 20 March 2008

Image:1hov.gif


PDB ID 1hov

Drag the structure with the mouse to rotate
Ligands: , and
Activity: Gelatinase A, with EC number 3.4.24.24
Coordinates: save as pdb, mmCIF, xml



SOLUTION STRUCTURE OF A CATALYTIC DOMAIN OF MMP-2 COMPLEXED WITH SC-74020


Contents

Overview

MMP-2 is a member of the matrix metalloproteinase family that has been implicated in tumor cell metastasis and angiogenesis. Here, we describe the solution structure of a catalytic domain of MMP-2 complexed with a hydroxamic acid inhibitor (SC-74020), determined by three-dimensional heteronuclear NMR spectroscopy. The catalytic domain, designated MMP-2C, has a short peptide linker replacing the internal fibronectin-domain insertion and is enzymatically active. Distance geometry-simulated annealing calculations yielded 14 converged structures with atomic root-mean-square deviations (r.m.s.d.) of 1.02 and 1.62 A from the mean coordinate positions for the backbone and for all heavy atoms, respectively, when 11 residues at the N-terminus are excluded. The structure has the same global fold as observed for other MMP catalytic domains and is similar to previously solved crystal structures of MMP-2. Differences observed between the solution and the crystal structures, near the bottom of the S1' specificity loop, appear to be induced by the large inhibitor present in the solution structure. The MMP-2C solution structure is compared with MMP-8 crystal structure bound to the same inhibitor to highlight the differences especially in the S1' specificity loop. The finding provides a structural explanation for the selectivity between MMP-2 and MMP-8 that is achieved by large inhibitors.

Disease

Known diseases associated with this structure: Osteolysis, idiopathic, Saudi type OMIM:[120360], Winchester syndrome OMIM:[120360]

About this Structure

1HOV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure and backbone dynamics of the catalytic domain of matrix metalloproteinase-2 complexed with a hydroxamic acid inhibitor., Feng Y, Likos JJ, Zhu L, Woodward H, Munie G, McDonald JJ, Stevens AM, Howard CP, De Crescenzo GA, Welsch D, Shieh HS, Stallings WC, Biochim Biophys Acta. 2002 Jul 29;1598(1-2):10-23. PMID:12147339

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