Residues forming a hydrophobic pocket in ARF3 are determinants of GDP dissociation and effector interactions

FEBS Letters

Kuai, Jun¹  Kahn, Richard A¹ 

[1] Department of Biochemistry, Emory University School of Medicine, 1510 Clifton Rd, Atlanta, GA 30322-3050, USA

关键词: ADP-ribosylation factor;    Regulatory GTPase;    Effector interaction;    Guanine nucleotide binding;   

DOI  :  10.1016/S0014-5793(00)02325-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Three residues of human ADP-ribosylation factor 3 (ARF3) (F51, W66 and Y81) cluster into a hydrophobic pocket in the inactive, GDP-bound protein. Disruption of the hydrophobic pocket with mutations at these residues increased the rate of GDP dissociation and association, but not always that of GTPγS. Several of the same mutants were found to be defective, often selectively, in binding different ARF effectors in two-hybrid assays. These results highlight three features of these hydrophobic residues in regulating (1) the rate of GDP dissociation, (2) the conformational changes that promote GTP binding and (3) their role in binding target proteins.

【 授权许可】

Unknown