2pbh: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2pbh.gif|left|200px]]<br />
-<applet load="2pbh" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2pbh, resolution 3.3&Aring;" />
-'''CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN B AT 3.3 ANGSTROM RESOLUTION'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN B AT 3.3 ANGSTROM RESOLUTION==
-A wild-type human procathepsin B was expressed, crystallized in two, crystal forms and its crystal structure determined at 3.2 and 3.3, Angstroms resolution. The structure reveals that the propeptide folds on, the cathepsin B surface, shielding the enzyme active site from exposure to, solvent. The structure of the enzymatically active domains is virtually, identical to that of the native enzyme [Musil et al. (1991) EMBO J. 10, 2321-2330]: the main difference is that the occluding loop residues are, lifted above the body of the mature enzyme, supporting the propeptide, structure.
+<StructureSection load='2pbh' size='340' side='right'caption='[[2pbh]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2pbh]] 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=2PBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PBH FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#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=2pbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pbh OCA], [https://pdbe.org/2pbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pbh RCSB], [https://www.ebi.ac.uk/pdbsum/2pbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pbh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CATB_HUMAN CATB_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 ==
+[[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/pb/2pbh_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=2pbh ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A wild-type human procathepsin B was expressed, crystallized in two crystal forms and its crystal structure determined at 3.2 and 3.3 Angstroms resolution. The structure reveals that the propeptide folds on the cathepsin B surface, shielding the enzyme active site from exposure to solvent. The structure of the enzymatically active domains is virtually identical to that of the native enzyme [Musil et al. (1991) EMBO J. 10, 2321-2330]: the main difference is that the occluding loop residues are lifted above the body of the mature enzyme, supporting the propeptide structure.
-==About this Structure==
+Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide.,Turk D, Podobnik M, Kuhelj R, Dolinar M, Turk V FEBS Lett. 1996 Apr 22;384(3):211-4. PMID:8617355<ref>PMID:8617355</ref>
-PBH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Cathepsin_B Cathepsin B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.1 3.4.22.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2PBH OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide., Turk D, Podobnik M, Kuhelj R, Dolinar M, Turk V, FEBS Lett. 1996 Apr 22;384(3):211-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8617355 8617355]
+</div>
-[[Category: Cathepsin B]]
+<div class="pdbe-citations 2pbh" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cathepsin 3D structures|Cathepsin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Kuhelj, R.]]
+[[Category: Kuhelj R]]
-[[Category: Podobnik, M.]]
+[[Category: Podobnik M]]
-[[Category: Turk, D.]]
+[[Category: Turk D]]
-[[Category: Turk, V.]]
+[[Category: Turk V]]
-[[Category: cathepsin b]]
-[[Category: crystal structure]]
-[[Category: cysteine protease]]
-[[Category: papain]]
-[[Category: proenzyme]]
-[[Category: thiol protease]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:22:12 2007''