Title : Identification of residues of the H-ras protein critical for functional interaction with guanine nucleotide exchange factors.

Pub. Date : 1994 Feb

PMID : 8289791






3 Functional Relationships(s)
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1 Most critically, a complex of Ras and CDC25 protein, unlike free Fas protein, possesses significantly greater affinity for GTP than for GDP. Guanosine Diphosphate Ras family guanine nucleotide exchange factor CDC25 Saccharomyces cerevisiae S288C
2 Furthermore, the Ras CDC25 complex is more readily dissociated into free subunits by GTP than it is by GDP. Guanosine Diphosphate Ras family guanine nucleotide exchange factor CDC25 Saccharomyces cerevisiae S288C
3 Both of these results suggest a function for CDC25 in promoting the selective exchange of GTP for GDP. Guanosine Diphosphate Ras family guanine nucleotide exchange factor CDC25 Saccharomyces cerevisiae S288C