Abstract:
:The GTPase-activating protein (GAP) stimulates the GTPase reaction of p21 by 5 orders of magnitude such that the kcat of the reaction is increased to 19 s-1. Mutations of residues in loop L1 (Gly-12 and Gly-13), in loop L2 (Thr-35 and Asp-38), and in loop L4 (Gln-61 and Glu-63) influence the reaction in different ways, but all of these mutant p21 proteins still form complexes with GAP. The C-terminal domain of the human GAP gene product, GAP334, which comprises residues 714 to 1047, is 20 times less active than full-length GAP on a molar basis and has a fourfold lower affinity. This finding indicates that the N terminus of GAP containing the SH2 domains modifies the interaction between the catalytic domain and p21.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Gideon P,John J,Frech M,Lautwein A,Clark R,Scheffler JE,Wittinghofer Adoi
10.1128/mcb.12.5.2050subject
Has Abstractpub_date
1992-05-01 00:00:00pages
2050-6issue
5eissn
0270-7306issn
1098-5549journal_volume
12pub_type
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