1zlh

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[[Image:1zlh.gif|left|200px]]<br /><applet load="1zlh" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zlh.gif|left|200px]]
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caption="1zlh, resolution 1.70&Aring;" />
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'''Crystal structure of the tick carboxypeptidase inhibitor in complex with bovine carboxypeptidase A'''<br />
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{{Structure
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|PDB= 1zlh |SIZE=350|CAPTION= <scene name='initialview01'>1zlh</scene>, resolution 1.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Carboxypeptidase_A Carboxypeptidase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.1 3.4.17.1]
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|GENE=
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}}
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'''Crystal structure of the tick carboxypeptidase inhibitor in complex with bovine carboxypeptidase A'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ZLH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] 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_A Carboxypeptidase A], 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZLH OCA].
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1ZLH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Rhipicephalus_bursa Rhipicephalus bursa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZLH OCA].
==Reference==
==Reference==
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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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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://www.ncbi.nlm.nih.gov/pubmed/15961103 15961103]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Carboxypeptidase A]]
[[Category: Carboxypeptidase A]]
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[[Category: inhibitor-metallocarboxypeptidase complex]]
[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:36:59 2008''

Revision as of 13:37, 20 March 2008


PDB ID 1zlh

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands:
Activity: Carboxypeptidase A, with EC number 3.4.17.1
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the tick carboxypeptidase inhibitor in complex with bovine carboxypeptidase A


Overview

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

1ZLH is a Protein complex structure of sequences from Bos taurus and Rhipicephalus bursa. Full crystallographic information is available from OCA.

Reference

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

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