1biw: Difference between revisions
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==DESIGN AND SYNTHESIS OF CONFORMATIONALLY-CONSTRAINED MMP INHIBITORS== | ==DESIGN AND SYNTHESIS OF CONFORMATIONALLY-CONSTRAINED MMP INHIBITORS== | ||
<StructureSection load='1biw' size='340' side='right' caption='[[1biw]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1biw' size='340' side='right' caption='[[1biw]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
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</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=S80:N1-HYDROXY-2-(3-HYDROXY-PROPYL)-3-ISOBUTYL-N4-[1-(2-METHOXY-ETHYL)-2-OXO-AZEPAN-3-YL]-SUCCINAMIDE'>S80</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </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=S80:N1-HYDROXY-2-(3-HYDROXY-PROPYL)-3-ISOBUTYL-N4-[1-(2-METHOXY-ETHYL)-2-OXO-AZEPAN-3-YL]-SUCCINAMIDE'>S80</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Stromelysin_1 Stromelysin 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.17 3.4.24.17] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Stromelysin_1 Stromelysin 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.17 3.4.24.17] </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=1biw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1biw OCA], [http://pdbe.org/1biw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1biw RCSB], [http://www.ebi.ac.uk/pdbsum/1biw 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=1biw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1biw OCA], [http://pdbe.org/1biw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1biw RCSB], [http://www.ebi.ac.uk/pdbsum/1biw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1biw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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</div> | </div> | ||
<div class="pdbe-citations 1biw" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1biw" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:58, 8 November 2017
DESIGN AND SYNTHESIS OF CONFORMATIONALLY-CONSTRAINED MMP INHIBITORSDESIGN AND SYNTHESIS OF CONFORMATIONALLY-CONSTRAINED MMP INHIBITORS
Structural highlights
Disease[MMP3_HUMAN] Defects in MMP3 are the cause of susceptibility to coronary heart disease type 6 (CHDS6) [MIM:614466]. A multifactorial disease characterized by an imbalance between myocardial functional requirements and the capacity of the coronary vessels to supply sufficient blood flow. Decreased capacity of the coronary vessels is often associated with thickening and loss of elasticity of the coronary arteries. Note=A polymorphism in the MMP3 promoter region is associated with the risk of coronary heart disease and myocardial infarction, due to lower MMP3 proteolytic activity and higher extracellular matrix deposition in atherosclerotic lesions.[1] [2] Function[MMP3_HUMAN] Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA novel series of conformationally constrained matrix metalloprotease inhibitors was identified. The potencies observed for these inhibitors were highly dependent upon the substitution pattern on the caprolactam ring as well as the succinate moiety. Design and synthesis of conformationally-constrained MMP inhibitors.,Natchus MG, Cheng M, Wahl CT, Pikul S, Almstead NG, Bradley RS, Taiwo YO, Mieling GE, Dunaway CM, Snider CE, McIver JM, Barnett BL, McPhail SJ, Anastasio MB, De B Bioorg Med Chem Lett. 1998 Aug 18;8(16):2077-80. PMID:9873489[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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