1by8: Difference between revisions

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-{{Seed}}
-[[Image:1by8.png|left|200px]]
-<!--
+==THE CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN K==
-The line below this paragraph, containing "STRUCTURE_1by8", creates the "Structure Box" on the page.
+<StructureSection load='1by8' size='340' side='right'caption='[[1by8]], [[Resolution|resolution]] 2.60&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'>[[1by8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BY8 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]] 2.6&#8491;</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1by8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1by8 OCA], [https://pdbe.org/1by8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1by8 RCSB], [https://www.ebi.ac.uk/pdbsum/1by8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1by8 ProSAT]</span></td></tr>
-{{STRUCTURE_1by8|  PDB=1by8  |  SCENE=  }}
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[https://omim.org/entry/265800 265800]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref> <ref>PMID:9529353</ref> <ref>PMID:10491211</ref> <ref>PMID:10878663</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN] 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/by/1by8_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1by8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cathepsin K is a cysteine protease present in human osteoclasts that plays an important role in bone resorption. Cathepsin K is synthesized as an inactive proenzyme and activated under conditions of low pH. Autoproteolytic processing of the N-terminal 99 amino acid propeptide produces the active, mature form of cathepsin K. It is presumed that the activation of procathepsin K in vivo occurs in the bone resorption pit, which has a low-pH environment. We have determined the structure of human procathepsin K at 2.8 A resolution. The structure of the mature enzyme domain within procathepsin K is virtually identical to that of mature cathepsin K. The fold of the propeptide of procathepsin K is similar to that observed in procathepsins B and L despite differences in length and sequence. A portion of the propeptide occupies the active site cleft of cathepsin K. Hydrophobic interactions, salt bridges, and hydrogen-bonding interactions are observed in the structure of the propeptide and between the propeptide and the mature enzyme of procathepsin K. These interactions suggest an explanation for the stability of the proenzyme. The structure of procathepsin K contributes to an understanding of the molecular basis of inhibition by the propeptide portion of the molecule and activation of this important member of the cysteine protease family.
-===THE CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN K===
+The crystal structure of human procathepsin K.,LaLonde JM, Zhao B, Janson CA, D'Alessio KJ, McQueney MS, Orsini MJ, Debouck CM, Smith WW Biochemistry. 1999 Jan 19;38(3):862-9. PMID:9893980<ref>PMID:9893980</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1by8" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_9893980}}, adds the Publication Abstract to the page
+*[[Cathepsin 3D structures|Cathepsin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 9893980 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9893980}}
+__TOC__
+</StructureSection>
-==About this Structure==
-BY8 is a 1 chain 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=1BY8 OCA].
-==Reference==
-<ref group="xtra">PMID:9893980</ref><references group="xtra"/>
-[[Category: Cathepsin K]]
 [[Category: Homo sapiens]]
-[[Category: Abdel-Mequid, S S.]]
+[[Category: Large Structures]]
-[[Category: Carr, T J.]]
+[[Category: Abdel-Mequid SS]]
-[[Category: Desjarlais, R L.]]
+[[Category: Carr TJ]]
-[[Category: Janson, C A.]]
+[[Category: Desjarlais RL]]
-[[Category: Lalonde, J M.]]
+[[Category: Janson CA]]
-[[Category: Smith, W W.]]
+[[Category: Lalonde JM]]
-[[Category: Thompson, S K.]]
+[[Category: Smith WW]]
-[[Category: Tomaszek, T A.]]
+[[Category: Thompson SK]]
-[[Category: Veber, D F.]]
+[[Category: Tomaszek TA]]
-[[Category: Yamashita, D S.]]
+[[Category: Veber DF]]
-[[Category: Zhao, B.]]
+[[Category: Yamashita DS]]
-[[Category: Papain]]
+[[Category: Zhao B]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:43:48 2009''