2ihs: Difference between revisions

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New page: left|200px<br /><applet load="2ihs" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ihs, resolution 2.2Å" /> '''Crystal structure of ...
 
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'''Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide'''<br />


==Overview==
==Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide==
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.
<StructureSection load='2ihs' size='340' side='right'caption='[[2ihs]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ihs]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IHS 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]] 2.2&#8491;</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=2ihs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ihs OCA], [https://pdbe.org/2ihs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ihs RCSB], [https://www.ebi.ac.uk/pdbsum/2ihs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ihs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GUS_DROME GUS_DROME] Involved in the localization of vas to the posterior pole of the oocyte. Required maternally in the germ line for efficient primordial germ cell formation.<ref>PMID:12479811</ref> <ref>PMID:20123973</ref>
== 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/ih/2ihs_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=2ihs ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:17189197</ref>
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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17189197 17189197]
</div>
<div class="pdbe-citations 2ihs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Oh, B.H.]]
[[Category: Oh BH]]
[[Category: Park, S.Y.]]
[[Category: Park SY]]
[[Category: Woo, J.S.]]
[[Category: Woo JS]]
[[Category: b30.2/spry]]
[[Category: f-box-spry]]
[[Category: gustavus]]
[[Category: spry-containing socs box]]
[[Category: trim family]]
[[Category: vasa]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:19:36 2007''

Latest revision as of 08:16, 17 October 2024

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

Structural highlights

2ihs is a 4 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GUS_DROME Involved in the localization of vas to the posterior pole of the oocyte. Required maternally in the germ line for efficient primordial germ cell formation.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Styhler S, Nakamura A, Lasko P. VASA localization requires the SPRY-domain and SOCS-box containing protein, GUSTAVUS. Dev Cell. 2002 Dec;3(6):865-76. PMID:12479811
  2. ↑ Kugler JM, Woo JS, Oh BH, Lasko P. Regulation of Drosophila vasa in vivo through paralogous cullin-RING E3 ligase specificity receptors. Mol Cell Biol. 2010 Apr;30(7):1769-82. doi: 10.1128/MCB.01100-09. Epub 2010 Feb, 1. PMID:20123973 doi:http://dx.doi.org/10.1128/MCB.01100-09
  3. ↑ Woo JS, Suh HY, Park SY, Oh BH. Structural basis for protein recognition by B30.2/SPRY domains. Mol Cell. 2006 Dec 28;24(6):967-76. PMID:17189197 doi:10.1016/j.molcel.2006.11.009

2ihs, resolution 2.20Å

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