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New page: left|200px<br /> <applet load="1zli" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zli, resolution 2.09Å" /> '''Crystal structure o...
 
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[[Image:1zli.gif|left|200px]]<br />
<applet load="1zli" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1zli, resolution 2.09&Aring;" />
'''Crystal structure of the tick carboxypeptidase inhibitor in complex with human carboxypeptidase B'''<br />


==Overview==
==Crystal structure of the tick carboxypeptidase inhibitor in complex with human carboxypeptidase B==
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.
<StructureSection load='1zli' size='340' side='right'caption='[[1zli]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CBPB1_HUMAN CBPB1_HUMAN]
== 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/zl/1zli_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=1zli ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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>
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 ZN 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZLI OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
[[Category: Carboxypeptidase B]]
<div class="pdbe-citations 1zli" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Rhipicephalus bursa]]
[[Category: Rhipicephalus bursa]]
[[Category: Arolas, J.L.]]
[[Category: Arolas JL]]
[[Category: Aviles, F.X.]]
[[Category: Aviles FX]]
[[Category: Holak, T.A.]]
[[Category: Holak TA]]
[[Category: Huber, R.]]
[[Category: Huber R]]
[[Category: Lorenzo, J.]]
[[Category: Lorenzo J]]
[[Category: Popowicz, G.M.]]
[[Category: Popowicz GM]]
[[Category: Sommerhoff, C.P.]]
[[Category: Sommerhoff CP]]
[[Category: ZN]]
[[Category: beta-defensin fold (tci)]]
[[Category: eight-stranded twisted beta-sheet surrounded by eight alpha-helices (cpb)]]
[[Category: inhibitor-metallocarboxypeptidase complex]]
 
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