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Article

The structural basis of the activation of Ras by Sos.

Nature - 23 Jul 1998

Boriack-Sjodin P A, Margarit S M, Bar-Sagi D, Kuriyan J

Abstract excerpt

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...

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Identifiers

PMID: 9690470
DOI: 10.1038/28548

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Related research

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Research trail→

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The structural basis of the activation of Ras by Sos.PMID 9690470Read ↗

Structural analysis of autoinhibition in the Ras activator Son of sevenless.Semantic proximity Read ↗

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Molecular assemblies of the catalytic domain of SOS with KRas and oncogenic mutants.Semantic proximity Read ↗

Basis for signaling specificity difference between Sos and Ras-GRF guanine nucleotide exchange factors.Semantic proximity Read ↗

New class of Son-of-sevenless (Sos) alleles highlights the complexities of Sos function.Semantic proximity Read ↗

Structural characterization of 14-3-3ζ in complex with the human Son of sevenless homolog 1 (SOS1).Semantic proximity Read ↗

The Son of sevenless gene product: a putative activator of Ras.Semantic proximity Read ↗

An SH3-SH2-SH3 protein is required for p21Ras1 activation and binds to sevenless and Sos proteins in vitro.Semantic proximity Read ↗

The Grb2 binding domain of mSos1 is not required for downstream signal transduction.Semantic proximity Read ↗

Characterization of a Ras mutant with identical GDP- and GTP-bound structures .Semantic proximity Read ↗

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