Abstract：
:The crystal structure of human H-Ras complexed with the Ras guanine-nucleotide-exchange-factor region of the Son of sevenless (Sos) protein has been determined at 2.8 A resolution. The normally tight interaction of nucleotides with Ras is disrupted by Sos in two ways. First, the insertion into Ras of an alpha-helix from Sos results in the displacement of the Switch 1 region of Ras, opening up the nucleotide-binding site. Second, side chains presented by this helix and by a distorted conformation of the Switch 2 region of Ras alter the chemical environment of the binding site for the phosphate groups of the nucleotide and the associated magnesium ion, so that their binding is no longer favoured. Sos does not impede the binding sites for the base and the ribose of GTP or GDP, so the Ras-Sos complex adopts a structure that allows nucleotide release and rebinding.
journal_name
Naturejournal_title
Natureauthors
Boriack-Sjodin PA,Margarit SM,Bar-Sagi D,Kuriyan Jdoi
10.1038/28548subject
Has Abstractpub_date
1998-07-23 00:00:00pages
337-43issue
6691eissn
0028-0836issn
1476-4687journal_volume
394pub_type
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