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New page: left|200px<br /><applet load="1k1z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k1z" /> '''Solution structure of N-terminal SH3 domain ...
 
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[[Image:1k1z.gif|left|200px]]<br /><applet load="1k1z" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Solution structure of N-terminal SH3 domain mutant(P33G) of murine Vav'''<br />


==Overview==
==Solution structure of N-terminal SH3 domain mutant(P33G) of murine Vav==
The three-dimensional structure of the N-terminal SH3 domain (residues, 583-660) of murine Vav, which contains a tetra-proline sequence (Pro, 607-Pro 610), was determined by NMR. The solution structure of the SH3, domain shows a typical SH3 fold, but it exists in two conformations due to, cis-trans isomerization at the Gly614-Pro615 bond. The NMR structure of, the P615G mutant, where Pro615 is replaced by glycine, reveals that the, tetra-proline region is inserted into the RT-loop and binds to its own SH3, structure. The C-terminal SH3 domain of Grb2 specifically binds to the, trans form of the N-terminal SH3 domain of Vav. The surface of Vav, N-terminal SH3 which binds to Grb2 C-terminal SH3 was elucidated by, chemical shift mapping experiments using NMR. The surface does not involve, the tetra-proline region but involves the region comprising the n-src, loop, the N-terminal and the C-terminal regions. This surface is located, opposite to the tetra-proline containing region, consistent with that of, our previous mutagenesis studies.
<StructureSection load='1k1z' size='340' side='right'caption='[[1k1z]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1k1z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K1Z FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1k1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k1z OCA], [https://pdbe.org/1k1z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k1z RCSB], [https://www.ebi.ac.uk/pdbsum/1k1z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k1z ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VAV_MOUSE VAV_MOUSE] Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation.
== 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/k1/1k1z_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1k1z ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of the N-terminal SH3 domain (residues 583-660) of murine Vav, which contains a tetra-proline sequence (Pro 607-Pro 610), was determined by NMR. The solution structure of the SH3 domain shows a typical SH3 fold, but it exists in two conformations due to cis-trans isomerization at the Gly614-Pro615 bond. The NMR structure of the P615G mutant, where Pro615 is replaced by glycine, reveals that the tetra-proline region is inserted into the RT-loop and binds to its own SH3 structure. The C-terminal SH3 domain of Grb2 specifically binds to the trans form of the N-terminal SH3 domain of Vav. The surface of Vav N-terminal SH3 which binds to Grb2 C-terminal SH3 was elucidated by chemical shift mapping experiments using NMR. The surface does not involve the tetra-proline region but involves the region comprising the n-src loop, the N-terminal and the C-terminal regions. This surface is located opposite to the tetra-proline containing region, consistent with that of our previous mutagenesis studies.


==About this Structure==
Solution structure of N-terminal SH3 domain of Vav and the recognition site for Grb2 C-terminal SH3 domain.,Ogura K, Nagata K, Horiuchi M, Ebisui E, Hasuda T, Yuzawa S, Nishida M, Hatanaka H, Inagaki F J Biomol NMR. 2002 Jan;22(1):37-46. PMID:11885979<ref>PMID:11885979</ref>
1K1Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K1Z OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of N-terminal SH3 domain of Vav and the recognition site for Grb2 C-terminal SH3 domain., Ogura K, Nagata K, Horiuchi M, Ebisui E, Hasuda T, Yuzawa S, Nishida M, Hatanaka H, Inagaki F, J Biomol NMR. 2002 Jan;22(1):37-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11885979 11885979]
</div>
<div class="pdbe-citations 1k1z" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Ebisui E]]
[[Category: Ebisui, E.]]
[[Category: Hasuda T]]
[[Category: Hasuda, T.]]
[[Category: Hatanaka H]]
[[Category: Hatanaka, H.]]
[[Category: Horiuchi M]]
[[Category: Horiuchi, M.]]
[[Category: Inagaki F]]
[[Category: Inagaki, F.]]
[[Category: Nagata K]]
[[Category: Nagata, K.]]
[[Category: Nishida M]]
[[Category: Nishida, M.]]
[[Category: Ogura K]]
[[Category: Ogura, K.]]
[[Category: Yuzawa S]]
[[Category: Yuzawa, S.]]
[[Category: proto-oncogene]]
[[Category: sh3]]
 
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Latest revision as of 18:12, 29 May 2024

Solution structure of N-terminal SH3 domain mutant(P33G) of murine Vav

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