Energetic aspects of intramolecular coupling between the nucleotide binding site and the distal switch II region of the yeast RAS2 protein.

Abstract:

:We have studied the interaction of the yeast RAS2 protein with guanine nucleotides using energetic parameters for the dissociation of RAS.nucleotide complexes. The results indicated that a Gly-->Ser substitution at position 82 led to an altered interaction with GppNHp and, to a lesser extent, also with GDP. It was also possible to conclude that structural perturbation of Gly82 can stimulate nucleotide release by decreasing the energetic barrier for nucleotide dissociation. This, together with the observation that residues 80 and 81 are involved in the response of RAS to nucleotide exchange factors without affecting GDP binding per se, suggests a potential mechanism for exchange factor-stimulated GDP release.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

De Vendittis E,Fasano O

doi

10.1016/0014-5793(94)00521-4

subject

Has Abstract

pub_date

1994-06-27 00:00:00

pages

133-6

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(94)00521-4

journal_volume

347

pub_type

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