2ihs

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(New page: 200px<br /><applet load="2ihs" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ihs, resolution 2.2&Aring;" /> '''Crystal structure of ...)
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caption="2ihs, resolution 2.2&Aring;" />
'''Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide'''<br />
'''Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide'''<br />
==Overview==
==Overview==
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B30.2/SPRY domains are found in numerous proteins that cover a wide, spectrum of biological functions, including regulation of cytokine, signaling and innate retroviral restriction. Herein, we report the crystal, structure of the B30.2/SPRY domain of a SPRY domain-containing SOCS box, (SSB) protein, GUSTAVUS, complexed with a 20 amino acid peptide derived, from the RNA helicase VASA, revealing how these domains recognize target, proteins. The peptide-binding site is conformationally rigid and has a, preformed pocket. The interaction between the pocket and the, Asp-Ile-Asn-Asn-Asn-Asn sequence within the peptide accounts for the, high-affinity binding between GUSTAVUS and VASA. This observation led to a, facile identification of the Glu-Leu-Asn-Asn-Asn-Leu sequence as the, recognition motif in a proapoptotic protein Par-4 for its interaction with, a GUSTAVUS homolog, SSB-1. Ensuing analyses indicated that many B30.2/SPRY, domains have a similar preformed pocket, which would allow them to bind, multiple targets.
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B30.2/SPRY domains are found in numerous proteins that cover a wide spectrum of biological functions, including regulation of cytokine signaling and innate retroviral restriction. Herein, we report the crystal structure of the B30.2/SPRY domain of a SPRY domain-containing SOCS box (SSB) protein, GUSTAVUS, complexed with a 20 amino acid peptide derived from the RNA helicase VASA, revealing how these domains recognize target proteins. The peptide-binding site is conformationally rigid and has a preformed pocket. The interaction between the pocket and the Asp-Ile-Asn-Asn-Asn-Asn sequence within the peptide accounts for the high-affinity binding between GUSTAVUS and VASA. This observation led to a facile identification of the Glu-Leu-Asn-Asn-Asn-Leu sequence as the recognition motif in a proapoptotic protein Par-4 for its interaction with a GUSTAVUS homolog, SSB-1. Ensuing analyses indicated that many B30.2/SPRY domains have a similar preformed pocket, which would allow them to bind multiple targets.
==About this Structure==
==About this Structure==
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2IHS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IHS OCA].
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2IHS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IHS OCA].
==Reference==
==Reference==
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[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Oh, B.H.]]
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[[Category: Oh, B H.]]
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[[Category: Park, S.Y.]]
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[[Category: Park, S Y.]]
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[[Category: Woo, J.S.]]
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[[Category: Woo, J S.]]
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[[Category: b30.2/spry]]
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[[Category: b30 2/spry]]
[[Category: f-box-spry]]
[[Category: f-box-spry]]
[[Category: gustavus]]
[[Category: gustavus]]
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[[Category: vasa]]
[[Category: vasa]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:19:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:50 2008''

Revision as of 15:52, 21 February 2008


2ihs, resolution 2.2Å

Drag the structure with the mouse to rotate

Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide

Overview

B30.2/SPRY domains are found in numerous proteins that cover a wide spectrum of biological functions, including regulation of cytokine signaling and innate retroviral restriction. Herein, we report the crystal structure of the B30.2/SPRY domain of a SPRY domain-containing SOCS box (SSB) protein, GUSTAVUS, complexed with a 20 amino acid peptide derived from the RNA helicase VASA, revealing how these domains recognize target proteins. The peptide-binding site is conformationally rigid and has a preformed pocket. The interaction between the pocket and the Asp-Ile-Asn-Asn-Asn-Asn sequence within the peptide accounts for the high-affinity binding between GUSTAVUS and VASA. This observation led to a facile identification of the Glu-Leu-Asn-Asn-Asn-Leu sequence as the recognition motif in a proapoptotic protein Par-4 for its interaction with a GUSTAVUS homolog, SSB-1. Ensuing analyses indicated that many B30.2/SPRY domains have a similar preformed pocket, which would allow them to bind multiple targets.

About this Structure

2IHS is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

Structural basis for protein recognition by B30.2/SPRY domains., Woo JS, Suh HY, Park SY, Oh BH, Mol Cell. 2006 Dec 28;24(6):967-76. PMID:17189197

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