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1k1z

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(New page: 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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'''Solution structure of N-terminal SH3 domain mutant(P33G) of murine Vav'''<br />
'''Solution structure of N-terminal SH3 domain mutant(P33G) of murine Vav'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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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].
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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://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1Z OCA].
==Reference==
==Reference==
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[[Category: sh3]]
[[Category: sh3]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:47:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:15 2008''

Revision as of 11:29, 21 February 2008

Image:1k1z.gif

1k1z

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

Overview

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

1K1Z is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

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

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