1ukm

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(New page: 200px<br /><applet load="1ukm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ukm, resolution 1.90&Aring;" /> '''Crystal structure of...)
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[[Image:1ukm.gif|left|200px]]<br /><applet load="1ukm" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ukm.gif|left|200px]]<br /><applet load="1ukm" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ukm, resolution 1.90&Aring;" />
caption="1ukm, resolution 1.90&Aring;" />
'''Crystal structure of EMS16, an Antagonist of collagen receptor integrin alpha2beta1 (GPIa/IIa)'''<br />
'''Crystal structure of EMS16, an Antagonist of collagen receptor integrin alpha2beta1 (GPIa/IIa)'''<br />
==Overview==
==Overview==
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Snake venoms contain a number of hemostatically active C-type lectin-like, proteins (CLPs), which affect the blood coagulation system, endothelial, cells, and platelets. CLPs have broad similarities in structure and, possess distinct biological functions. EMS16, a CLP from Echis, multisquamatus venom, which is a potent and selective inhibitor of the, collagen receptor, glycoprotein Ia/IIa (integrin alpha2beta1), has been, used in the present study to examine structure-function relationships in, venom CLPs by X-ray crystallography. The structure of EMS16, determined at, a resolution of 1.9 A, revealed a heterodimer involved with domain, swapping of the central loop as observed in the structures of other CLPs., A part of the glycan was observed and identified as N-acetyl-D-glucosamine, (GlcNAc) in the electron density map at Asn21 of subunit B, an expected, glycosylation site. EMS16 had a unique, positively charged electrostatic, potential patch on the concave surface that may qualify as a site for, interaction with the I-domain of the glycoprotein Ia/IIa.
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Snake venoms contain a number of hemostatically active C-type lectin-like proteins (CLPs), which affect the blood coagulation system, endothelial cells, and platelets. CLPs have broad similarities in structure and possess distinct biological functions. EMS16, a CLP from Echis multisquamatus venom, which is a potent and selective inhibitor of the collagen receptor, glycoprotein Ia/IIa (integrin alpha2beta1), has been used in the present study to examine structure-function relationships in venom CLPs by X-ray crystallography. The structure of EMS16, determined at a resolution of 1.9 A, revealed a heterodimer involved with domain swapping of the central loop as observed in the structures of other CLPs. A part of the glycan was observed and identified as N-acetyl-D-glucosamine (GlcNAc) in the electron density map at Asn21 of subunit B, an expected glycosylation site. EMS16 had a unique, positively charged electrostatic potential patch on the concave surface that may qualify as a site for interaction with the I-domain of the glycoprotein Ia/IIa.
==About this Structure==
==About this Structure==
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1UKM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Echis_multisquamatus Echis multisquamatus] with NAG, CL and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UKM OCA].
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1UKM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Echis_multisquamatus Echis multisquamatus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UKM OCA].
==Reference==
==Reference==
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[[Category: domain swapping]]
[[Category: domain swapping]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:08:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:33 2008''

Revision as of 13:25, 21 February 2008

Image:1ukm.gif

1ukm, resolution 1.90Å

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Crystal structure of EMS16, an Antagonist of collagen receptor integrin alpha2beta1 (GPIa/IIa)

Overview

Snake venoms contain a number of hemostatically active C-type lectin-like proteins (CLPs), which affect the blood coagulation system, endothelial cells, and platelets. CLPs have broad similarities in structure and possess distinct biological functions. EMS16, a CLP from Echis multisquamatus venom, which is a potent and selective inhibitor of the collagen receptor, glycoprotein Ia/IIa (integrin alpha2beta1), has been used in the present study to examine structure-function relationships in venom CLPs by X-ray crystallography. The structure of EMS16, determined at a resolution of 1.9 A, revealed a heterodimer involved with domain swapping of the central loop as observed in the structures of other CLPs. A part of the glycan was observed and identified as N-acetyl-D-glucosamine (GlcNAc) in the electron density map at Asn21 of subunit B, an expected glycosylation site. EMS16 had a unique, positively charged electrostatic potential patch on the concave surface that may qualify as a site for interaction with the I-domain of the glycoprotein Ia/IIa.

About this Structure

1UKM is a Protein complex structure of sequences from Echis multisquamatus with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structural characterization of EMS16, an antagonist of collagen receptor (GPIa/IIa) from the venom of Echis multisquamatus., Horii K, Okuda D, Morita T, Mizuno H, Biochemistry. 2003 Nov 4;42(43):12497-502. PMID:14580195

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