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1hdu

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(New page: 200px<br /> <applet load="1hdu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hdu, resolution 1.75&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1hdu.gif|left|200px]]<br />
 
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<applet load="1hdu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hdu, resolution 1.75&Aring;" />
 
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'''CRYSTAL STRUCTURE OF BOVINE PANCREATIC CARBOXYPEPTIDASE A COMPLEXED WITH AMINOCARBONYLPHENYLALANINE AT 1.75 A'''<br />
 
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==Overview==
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==Crystal structure of bovine pancreatic carboxypeptidase A complexed with aminocarbonylphenylalanine at 1.75 A==
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Both D- and L-isomers of N-(hydroxyaminocarbonyl)phenylalanine () were, shown to have strong binding affinity towards carboxypeptidase A (CPA), with D- being more potent than its enantiomer by 3-fold (Chung, S. J.;, Kim, D. H. Bioorg. Med. Chem. 2001, 9, 185.). In order to understand the, reversed stereochemical preference shown in the CPA inhibition, we have, solved the crystal structures of CPA complexed with each enantiometer of, up to 1.75 A resolution. Inhibitor L- whose stereochemistry belongs to the, stereochemical series of substrate binds CPA like substrate does with its, carbonyl oxygen coordinating to the active site zinc ion. Its hydroxyl is, engaged in hydrogen bonding with the carboxylate of Glu-270. On the other, hand, in binding of D- to CPA, its terminal hydroxyl group is ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11937361 (full description)]]
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<StructureSection load='1hdu' size='340' side='right'caption='[[1hdu]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hdu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HDU FirstGlance]. <br>
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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]] 1.75&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ING:D-[(AMINO)CARBONYL]PHENYLALANINE'>ING</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1hdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hdu OCA], [https://pdbe.org/1hdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hdu RCSB], [https://www.ebi.ac.uk/pdbsum/1hdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hdu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CBPA1_BOVIN CBPA1_BOVIN] Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hd/1hdu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1hdu ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1HDU is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]] with ZN and ING as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.1 3.4.17.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HDU OCA]].
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Insight into the stereochemistry in the inhibition of carboxypeptidase A with N-(hydroxyaminocarbonyl)phenylalanine: binding modes of an enantiomeric pair of the inhibitor to carboxypeptidase A., Cho JH, Kim DH, Chung SJ, Ha NC, Oh BH, Yong Choi K, Bioorg Med Chem. 2002 Jun;10(6):2015-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11937361 11937361]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cho, J.H.]]
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[[Category: Cho JH]]
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[[Category: Choi, K.Y.]]
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[[Category: Choi KY]]
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[[Category: Chung, S.J.]]
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[[Category: Chung SJ]]
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[[Category: Ha, N.C.]]
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[[Category: Ha N-C]]
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[[Category: Kim, D.H.]]
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[[Category: Kim DH]]
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[[Category: Oh, B.H.]]
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[[Category: Oh B-H]]
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[[Category: ING]]
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[[Category: ZN]]
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[[Category: cpa]]
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[[Category: inhibitor]]
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[[Category: lbhb]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:28:07 2007''
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Current revision

Crystal structure of bovine pancreatic carboxypeptidase A complexed with aminocarbonylphenylalanine at 1.75 A

PDB ID 1hdu

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