2f7d: Difference between revisions

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-[[Image:2f7d.png|left|200px]]
-<!--
+==A mutant rabbit cathepsin K with a nitrile inhibitor==
-The line below this paragraph, containing "STRUCTURE_2f7d", creates the "Structure Box" on the page.
+<StructureSection load='2f7d' size='340' side='right'caption='[[2f7d]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2f7d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F7D FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NOQ:(1R,2R)-N-(2-AMINOETHYL)-2-{[(4-METHOXYPHENYL)SULFONYL]METHYL}CYCLOHEXANECARBOXAMIDE'>NOQ</scene></td></tr>
-{{STRUCTURE_2f7d|  PDB=2f7d  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f7d OCA], [https://pdbe.org/2f7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f7d RCSB], [https://www.ebi.ac.uk/pdbsum/2f7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f7d ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CATK_RABIT CATK_RABIT] Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f7/2f7d_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2f7d ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A new series of nonpeptidic cathepsin K inhibitors that are based on a beta-substituted cyclohexanecarboxamide motif has been developed. Lead optimization yielded compounds with sub-nanomolar potency and exceptional selectivity profiles against cathepsins B, L, and S. Use of fluorine atoms to block metabolism on the cyclohexyl ring led to compounds with excellent pharmacokinetic properties. Considering the well-established role of cathepsin K in osteoclast-mediated bone turnover, compounds such as (-)-34a (hrab Cat K IC(50) 0.28 nM; &gt;800-fold selectivity vs Cat B, L, and S; PK data in dogs: F 55%, t(1/2) = 15 h) exhibit great potential for development as an orally bioavailable therapeutic for treatment of diseases that involve bone loss.
-===A mutant rabbit cathepsin K with a nitrile inhibitor===
+Beta-substituted cyclohexanecarboxamide: a nonpeptidic framework for the design of potent inhibitors of cathepsin K.,Crane SN, Black WC, Palmer JT, Davis DE, Setti E, Robichaud J, Paquet J, Oballa RM, Bayly CI, McKay DJ, Somoza JR, Chauret N, Seto C, Scheigetz J, Wesolowski G, Masse F, Desmarais S, Ouellet M J Med Chem. 2006 Feb 9;49(3):1066-79. PMID:16451072<ref>PMID:16451072</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_16451072}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2f7d" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16451072 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_16451072}}
-==About this Structure==
-[[2f7d]] is a 1 chain structure of [[Cathepsin]] with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F7D OCA].
 ==See Also==
-*[[Cathepsin]]
+*[[Cathepsin 3D structures|Cathepsin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:16451072</ref><references group="xtra"/>
+__TOC__
-[[Category: Cathepsin K]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Somoza, J R.]]
+[[Category: Somoza JR]]
-[[Category: Hydrolase]]
-[[Category: Papain cysteine protease]]