1K1Z

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

Summary for 1K1Z

• Entry DOI: 10.2210/pdb1k1z/pdb
• NMR Information: BMRB: 5179
• Descriptor: vav (1 entity in total)
• Functional Keywords: sh3, proto-oncogene, signaling protein
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 1
• Total formula weight: 8990.08

Authors

Ogura, K.,Nagata, K.,Horiuchi, M.,Ebisui, E.,Hasuda, T.,Yuzawa, S.,Nishida, M.,Hatanaka, H.,Inagaki, F. (deposition date: 2001-09-26, release date: 2001-10-10, Last modification date: 2024-05-29)

Primary citation

Ogura, K.,Nagata, K.,Horiuchi, M.,Ebisui, E.,Hasuda, T.,Yuzawa, S.,Nishida, M.,Hatanaka, H.,Inagaki, F.
Solution structure of N-terminal SH3 domain of Vav and the recognition site for Grb2 C-terminal SH3 domain
J.BIOMOL.NMR, 22:37-46, 2002

PubMed Abstract: 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.

PubMed: 11885979
DOI: 10.1023/A:1013868731495

Experimental method

SOLUTION NMR