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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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