title: Solution structure of the SH3 domain of DOCK180.
abstract: DOCK180 family proteins are Rho guanine nucleotide exchange factors. DOCK1-5 contains an N-terminal SH3 domain implicated in their autoinhibition. Release of the closed conformation requires the interaction between SH3 and engulfment and cell motility (ELMO). Here, we solved the solution structure of DOCK180 SH3 domain, which shares similar target binding features with the SH3 domain of DOCK2. The conserved N-terminal extension packs with the SH3 core domain and forms a new target binding site distinct from the canonical "PxxP" site. Our results demonstrate that the bidentate target binding mode of DOCK180 SH3 domain might be a general feature in all DOCK proteins.
authors.affiliation: Key Laboratory of Molecular Medicine, Ministry of Education, Department of Biochemistry and Molecular Biology, Shanghai Medical College, Fudan University, Shanghai, People's Republic of China.
authors.forename: Xiangrong
authors.initials: X
authors.lastname: Liu
authors.forename: Fengjuan
authors.initials: F
authors.lastname: Li
authors.forename: Zhu
authors.initials: Z
authors.lastname: Pan
authors.forename: Wenning
authors.initials: W
authors.lastname: Wang
authors.forename: Wenyu
authors.initials: W
authors.lastname: Wen
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D016415:Sequence Alignment; D020744:rac GTP-Binding Proteins / Q000737:chemistry*; D018909:src Homology Domains
chemical_list: C099818:DOCK1 protein, human; D020744:rac GTP-Binding Proteins