1yp1

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(New page: 200px<br /><applet load="1yp1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yp1, resolution 1.9&Aring;" /> '''Crystal structure of ...)
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caption="1yp1, resolution 1.9&Aring;" />
'''Crystal structure of a non-hemorrhagic fibrin(ogen)olytic metalloproteinase from venom of Agkistrodon acutus'''<br />
'''Crystal structure of a non-hemorrhagic fibrin(ogen)olytic metalloproteinase from venom of Agkistrodon acutus'''<br />
==Overview==
==Overview==
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Thrombotic occlusive diseases pose a great threat to human health., Thrombolytic agents are in widespread use for the dissolution of arterial, and venous pathologic thrombi in these kinds of diseases. Snake venom, metalloproteinases (SVMPs) can act directly on fibrin/fibrinogen and are, therefore potential candidates for therapeutic use against thrombotic, occlusive diseases. In this study, we have determined the crystal, structure of FII, a novel non-hemorrhagic SVMP isolated from Anhui, Agkistrodon acutus snake venom by molecular replacement. The structure, reveals that FII is a member of the P-I class SVMPs. The Zn2+ ion, essential for hydrolytic activity is found in the active site and is, tetrahedrally co-ordinated by three histidine residues and water molecule., Unambiguous electron density for a tri-peptide with sequence KNL is also, found located near the active site. Biochemical evidences show that the, tri-peptide KNL can inhibit the enzymatic activity of FII.
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Thrombotic occlusive diseases pose a great threat to human health. Thrombolytic agents are in widespread use for the dissolution of arterial and venous pathologic thrombi in these kinds of diseases. Snake venom metalloproteinases (SVMPs) can act directly on fibrin/fibrinogen and are therefore potential candidates for therapeutic use against thrombotic occlusive diseases. In this study, we have determined the crystal structure of FII, a novel non-hemorrhagic SVMP isolated from Anhui Agkistrodon acutus snake venom by molecular replacement. The structure reveals that FII is a member of the P-I class SVMPs. The Zn2+ ion essential for hydrolytic activity is found in the active site and is tetrahedrally co-ordinated by three histidine residues and water molecule. Unambiguous electron density for a tri-peptide with sequence KNL is also found located near the active site. Biochemical evidences show that the tri-peptide KNL can inhibit the enzymatic activity of FII.
==About this Structure==
==About this Structure==
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1YP1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinagkistrodon_acutus Deinagkistrodon acutus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YP1 OCA].
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1YP1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinagkistrodon_acutus Deinagkistrodon acutus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YP1 OCA].
==Reference==
==Reference==
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[[Category: fii crystal structure]]
[[Category: fii crystal structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:27:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:37 2008''

Revision as of 14:07, 21 February 2008


1yp1, resolution 1.9Å

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Crystal structure of a non-hemorrhagic fibrin(ogen)olytic metalloproteinase from venom of Agkistrodon acutus

Overview

Thrombotic occlusive diseases pose a great threat to human health. Thrombolytic agents are in widespread use for the dissolution of arterial and venous pathologic thrombi in these kinds of diseases. Snake venom metalloproteinases (SVMPs) can act directly on fibrin/fibrinogen and are therefore potential candidates for therapeutic use against thrombotic occlusive diseases. In this study, we have determined the crystal structure of FII, a novel non-hemorrhagic SVMP isolated from Anhui Agkistrodon acutus snake venom by molecular replacement. The structure reveals that FII is a member of the P-I class SVMPs. The Zn2+ ion essential for hydrolytic activity is found in the active site and is tetrahedrally co-ordinated by three histidine residues and water molecule. Unambiguous electron density for a tri-peptide with sequence KNL is also found located near the active site. Biochemical evidences show that the tri-peptide KNL can inhibit the enzymatic activity of FII.

About this Structure

1YP1 is a Protein complex structure of sequences from Deinagkistrodon acutus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a non-hemorrhagic fibrin(ogen)olytic metalloproteinase complexed with a novel natural tri-peptide inhibitor from venom of Agkistrodon acutus., Lou Z, Hou J, Liang X, Chen J, Qiu P, Liu Y, Li M, Rao Z, Yan G, J Struct Biol. 2005 Dec;152(3):195-203. Epub 2005 Nov 16. PMID:16330227

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