1zli

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[[Image:1zli.gif|left|200px]]<br /><applet load="1zli" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1zli, resolution 2.09&Aring;" />
 
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'''Crystal structure of the tick carboxypeptidase inhibitor in complex with human carboxypeptidase B'''<br />
 
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==Overview==
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==Crystal structure of the tick carboxypeptidase inhibitor in complex with human carboxypeptidase B==
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<StructureSection load='1zli' size='340' side='right'caption='[[1zli]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1zli]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rhipicephalus_bursa Rhipicephalus bursa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZLI 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]] 2.09&#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=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=1zli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zli OCA], [https://pdbe.org/1zli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zli RCSB], [https://www.ebi.ac.uk/pdbsum/1zli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zli ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CBPB1_HUMAN CBPB1_HUMAN]
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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/zl/1zli_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1zli ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
The tick carboxypeptidase inhibitor (TCI) is a proteinaceous inhibitor of metallo-carboxypeptidases present in the blood-sucking tick Rhipicephalus bursa. The three-dimensional crystal structures of recombinant TCI bound to bovine carboxypeptidase A and to human carboxypeptidase B have been determined and refined at 1.7 A and at 2.0 A resolution, respectively. TCI consists of two domains that are structurally similar despite the low degree of sequence homology. The domains, each consisting of a short alpha-helix followed by a small twisted antiparallel beta-sheet, show a high level of structural homology to proteins of the beta-defensin-fold family. TCI anchors to the surface of mammalian carboxypeptidases in a double-headed manner not previously seen for carboxypeptidase inhibitors: the last three carboxy-terminal amino acid residues interact with the active site of the enzyme in a way that mimics substrate binding, and the N-terminal domain binds to an exosite distinct from the active-site groove. The structures of these complexes should prove valuable in the applications of TCI as a thrombolytic drug and as a basis for the design of novel bivalent carboxypeptidase inhibitors.
The tick carboxypeptidase inhibitor (TCI) is a proteinaceous inhibitor of metallo-carboxypeptidases present in the blood-sucking tick Rhipicephalus bursa. The three-dimensional crystal structures of recombinant TCI bound to bovine carboxypeptidase A and to human carboxypeptidase B have been determined and refined at 1.7 A and at 2.0 A resolution, respectively. TCI consists of two domains that are structurally similar despite the low degree of sequence homology. The domains, each consisting of a short alpha-helix followed by a small twisted antiparallel beta-sheet, show a high level of structural homology to proteins of the beta-defensin-fold family. TCI anchors to the surface of mammalian carboxypeptidases in a double-headed manner not previously seen for carboxypeptidase inhibitors: the last three carboxy-terminal amino acid residues interact with the active site of the enzyme in a way that mimics substrate binding, and the N-terminal domain binds to an exosite distinct from the active-site groove. The structures of these complexes should prove valuable in the applications of TCI as a thrombolytic drug and as a basis for the design of novel bivalent carboxypeptidase inhibitors.
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==About this Structure==
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The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode.,Arolas JL, Popowicz GM, Lorenzo J, Sommerhoff CP, Huber R, Aviles FX, Holak TA J Mol Biol. 2005 Jul 15;350(3):489-98. PMID:15961103<ref>PMID:15961103</ref>
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1ZLI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rhipicephalus_bursa Rhipicephalus bursa] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Carboxypeptidase_B Carboxypeptidase B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.2 3.4.17.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZLI OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode., Arolas JL, Popowicz GM, Lorenzo J, Sommerhoff CP, Huber R, Aviles FX, Holak TA, J Mol Biol. 2005 Jul 15;350(3):489-98. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15961103 15961103]
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</div>
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[[Category: Carboxypeptidase B]]
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<div class="pdbe-citations 1zli" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
[[Category: Rhipicephalus bursa]]
[[Category: Rhipicephalus bursa]]
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[[Category: Arolas, J L.]]
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[[Category: Arolas JL]]
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[[Category: Aviles, F X.]]
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[[Category: Aviles FX]]
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[[Category: Holak, T A.]]
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[[Category: Holak TA]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Lorenzo, J.]]
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[[Category: Lorenzo J]]
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[[Category: Popowicz, G M.]]
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[[Category: Popowicz GM]]
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[[Category: Sommerhoff, C P.]]
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[[Category: Sommerhoff CP]]
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[[Category: ZN]]
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[[Category: beta-defensin fold (tci)]]
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[[Category: eight-stranded twisted beta-sheet surrounded by eight alpha-helices (cpb)]]
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[[Category: inhibitor-metallocarboxypeptidase complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:43 2008''
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Current revision

Crystal structure of the tick carboxypeptidase inhibitor in complex with human carboxypeptidase B

PDB ID 1zli

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