Title : Comparison of the predicted structures of loops in the ras-SOS protein bound to a single ras-p21 protein with the crystallographically determined structures in SOS bound to two ras-p21 proteins.

Pub. Date : 2005 Aug

PMID : 16323045






2 Functional Relationships(s)
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1 We have previously computed the structures of three loops, residues 591-596, 654-675 and 742-751, in the ras-p21 protein-binding domain (residues 568-1044) of the guanine nucleotide-exchange-promoting SOS protein that were crystallographically undefined when one molecule of ras-p21 (unbound to nucleotide) binds to SOS. Guanine Nucleotides H3 histone pseudogene 16 Homo sapiens
2 We have previously computed the structures of three loops, residues 591-596, 654-675 and 742-751, in the ras-p21 protein-binding domain (residues 568-1044) of the guanine nucleotide-exchange-promoting SOS protein that were crystallographically undefined when one molecule of ras-p21 (unbound to nucleotide) binds to SOS. Guanine Nucleotides H3 histone pseudogene 16 Homo sapiens