3s0n
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3s0n]] 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=3S0N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S0N FirstGlance]. <br> | <table><tr><td colspan='2'>[[3s0n]] 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=3S0N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S0N FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0BB:4-{3-[(4-METHYL-1-BENZOTHIOPHEN-3-YL)METHYL]-2-OXO-2,3-DIHYDRO-1H-BENZIMIDAZOL-1-YL}BUTANOIC+ACID'>0BB</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=0BB:4-{3-[(4-METHYL-1-BENZOTHIOPHEN-3-YL)METHYL]-2-OXO-2,3-DIHYDRO-1H-BENZIMIDAZOL-1-YL}BUTANOIC+ACID'>0BB</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CMA1, CYH, CYM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CMA1, CYH, CYM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> |
- | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chymase Chymase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.39 3.4.21.39] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chymase Chymase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.39 3.4.21.39] </span></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=3s0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s0n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s0n RCSB], [http://www.ebi.ac.uk/pdbsum/3s0n 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=3s0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s0n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s0n RCSB], [http://www.ebi.ac.uk/pdbsum/3s0n PDBsum]</span></td></tr> |
- | <table> | + | </table> |
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/CMA1_HUMAN CMA1_HUMAN]] Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Benzimidazolone as potent chymase inhibitor: Modulation of reactive metabolite formation in the hydrophobic (P(1)) region.,Lo HY, Nemoto PA, Kim JM, Hao MH, Qian KC, Farrow NA, Albaugh DR, Fowler DM, Schneiderman RD, Michael August E, Martin L, Hill-Drzewi M, Pullen SS, Takahashi H, De Lombaert S Bioorg Med Chem Lett. 2011 Aug 1;21(15):4533-9. Epub 2011 Jun 17. PMID:21733690<ref>PMID:21733690</ref> | Benzimidazolone as potent chymase inhibitor: Modulation of reactive metabolite formation in the hydrophobic (P(1)) region.,Lo HY, Nemoto PA, Kim JM, Hao MH, Qian KC, Farrow NA, Albaugh DR, Fowler DM, Schneiderman RD, Michael August E, Martin L, Hill-Drzewi M, Pullen SS, Takahashi H, De Lombaert S Bioorg Med Chem Lett. 2011 Aug 1;21(15):4533-9. Epub 2011 Jun 17. PMID:21733690<ref>PMID:21733690</ref> | ||
- | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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[[Category: Chymase]] | [[Category: Chymase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Farrow, N A | + | [[Category: Farrow, N A]] |
- | [[Category: Padyana, A K | + | [[Category: Padyana, A K]] |
- | [[Category: Qian, K C | + | [[Category: Qian, K C]] |
[[Category: Hydrolase-hydrolase inhibitor complex]] | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
[[Category: Serine protease]] | [[Category: Serine protease]] |
Revision as of 10:24, 25 December 2014
Crystal Structure of Human Chymase with Benzimidazolone Inhibitor
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