1m6d: Difference between revisions
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<StructureSection load='1m6d' size='340' side='right' caption='[[1m6d]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1m6d' size='340' side='right' caption='[[1m6d]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1m6d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1m6d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M6D FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYP:4-MORPHOLIN-4-YL-PIPERIDINE-1-CARBOXYLIC+ACID+[1-(3-BENZENESULFONYL-1-PROPYL-ALLYLCARBAMOYL)-2-PHENYLETHYL]-AMIDE'>MYP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYP:4-MORPHOLIN-4-YL-PIPERIDINE-1-CARBOXYLIC+ACID+[1-(3-BENZENESULFONYL-1-PROPYL-ALLYLCARBAMOYL)-2-PHENYLETHYL]-AMIDE'>MYP</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CATF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CATF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_F Cathepsin F], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.41 3.4.22.41] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_F Cathepsin F], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.41 3.4.22.41] </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=1m6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m6d RCSB], [http://www.ebi.ac.uk/pdbsum/1m6d 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=1m6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6d OCA], [http://pdbe.org/1m6d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m6d RCSB], [http://www.ebi.ac.uk/pdbsum/1m6d PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1m6d" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Cathepsin F]] | [[Category: Cathepsin F]] | ||
[[Category: | [[Category: Human]] | ||
[[Category: Ho, J D]] | [[Category: Ho, J D]] | ||
[[Category: Palmer, J T]] | [[Category: Palmer, J T]] | ||
Revision as of 12:37, 11 September 2015
Crystal structure of human cathepsin FCrystal structure of human cathepsin F
Structural highlights
Function[CATF_HUMAN] Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. 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 PubMedCathepsin F is a lysosomal cysteine protease of the papain family, and likely plays a regulatory role in processing the invariant chain that is associated with the major histocompatibility complex (MHC) class II. Evidence suggests that inhibiting cathepsin F activity will block MHC class II processing in macrophages. Consequently, inhibitors of this enzyme may be useful in treating certain diseases that involve an inappropriate or excessive immune response. We have determined the 1.7A structure of the mature domain of human cathepsin F associated with an irreversible vinyl sulfone inhibitor. This structure provides a basis for understanding cathepsin F's substrate specificity, and suggests ways of identifying potent and selective inhibitors of this enzyme. The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators.,Somoza JR, Palmer JT, Ho JD J Mol Biol. 2002 Sep 20;322(3):559-68. PMID:12225749[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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