1K4U

Solution structure of the C-terminal SH3 domain of p67phox complexed with the C-terminal tail region of p47phox

Summary for 1K4U

• Entry DOI: 10.2210/pdb1k4u/pdb
• NMR Information: BMRB: 5498
• Descriptor: PHAGOCYTE NADPH OXIDASE SUBUNIT P67PHOX, PHAGOCYTE NADPH OXIDASE SUBUNIT P47PHOX (2 entities in total)
• Functional Keywords: p67phox, p47phox, sh3-peptide complex, helix-turn-helix, hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P19878 P14598
• Total number of polymer chains: 2
• Total formula weight: 10361.70

Authors

Kami, K.,Takeya, R.,Sumimoto, H.,Kohda, D. (deposition date: 2001-10-08, release date: 2002-04-08, Last modification date: 2024-05-29)

Primary citation

Kami, K.,Takeya, R.,Sumimoto, H.,Kohda, D.
Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p.
EMBO J., 21:4268-4276, 2002

PubMed Abstract: The basic function of the Src homology 3 (SH3) domain is considered to be binding to proline-rich sequences containing a PxxP motif. Recently, many SH3 domains, including those from Grb2 and Pex13p, were reported to bind sequences lacking a PxxP motif. We report here that the 22 residue peptide lacking a PxxP motif, derived from p47(phox), binds to the C-terminal SH3 domain from p67(phox). We applied the NMR cross-saturation method to locate the interaction sites for the non-PxxP peptides on their cognate SH3 domains from p67(phox), Grb2 and Pex13p. The binding site of the Grb2 SH3 partially overlapped the conventional PxxP-binding site, whereas those of p67(phox) and Pex13p SH3s are located in different surface regions. The non-PxxP peptide from p47(phox) binds to the p67(phox) SH3 more tightly when it extends to the N-terminus to include a typical PxxP motif, which enabled the structure determination of the complex, to reveal that the non-PxxP peptide segment interacted with the p67(phox) SH3 in a compact helix-turn-helix structure (PDB entry 1K4U).

PubMed: 12169629
DOI: 10.1093/emboj/cdf428

Experimental method

SOLUTION NMR