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Residues forming a hydrophobic pocket in ARF3 are determinants of GDP dissociation and effector interactions
Author(s) -
Kuai Jun,
Kahn Richard A
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02325-5
Subject(s) - effector , chemistry , dissociation (chemistry) , hydrophobic effect , biochemistry , plasma protein binding , mutant , biophysics , guanosine diphosphate , gtp' , biology , guanosine triphosphate , organic chemistry , gene , enzyme
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.