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2pbh

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==CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN B AT 3.3 ANGSTROM RESOLUTION==
==CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN B AT 3.3 ANGSTROM RESOLUTION==
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<StructureSection load='2pbh' size='340' side='right' caption='[[2pbh]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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<StructureSection load='2pbh' size='340' side='right'caption='[[2pbh]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2pbh]] is a 1 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=2PBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PBH FirstGlance]. <br>
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<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>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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</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>
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<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=2pbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pbh OCA], [http://pdbe.org/2pbh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pbh RCSB], [http://www.ebi.ac.uk/pdbsum/2pbh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pbh ProSAT]</span></td></tr>
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<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>
</table>
== Function ==
== Function ==
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[[http://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.
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2pbh" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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*[[Cathepsin|Cathepsin]]
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*[[Cathepsin 3D structures|Cathepsin 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cathepsin B]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
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[[Category: Kuhelj, R]]
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[[Category: Kuhelj R]]
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[[Category: Podobnik, M]]
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[[Category: Podobnik M]]
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[[Category: Turk, D]]
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[[Category: Turk D]]
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[[Category: Turk, V]]
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[[Category: Turk V]]
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[[Category: Cathepsin b]]
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[[Category: Cysteine protease]]
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[[Category: Papain]]
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[[Category: Proenzyme]]
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[[Category: Thiol protease]]
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CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN B AT 3.3 ANGSTROM RESOLUTION

PDB ID 2pbh

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