Works (1)

Updated: July 5th, 2023 15:57

2004 journal article

Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap

STRUCTURE, 12(11), 2025–2036.

By: N. Nicely n, J. Kosak n, V. Serrano n & C. Mattos n

MeSH headings : Amino Acid Sequence; Binding Sites; Catalytic Domain; Crystallography, X-Ray; Guanosine Diphosphate / chemistry; Guanosine Diphosphate / metabolism; Guanosine Triphosphate / analogs & derivatives; Guanosine Triphosphate / chemistry; Guanosine Triphosphate / metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Sequence Homology, Amino Acid; rap GTP-Binding Proteins / chemistry; rap GTP-Binding Proteins / metabolism; ras Proteins / chemistry; ras Proteins / metabolism
TL;DR: Clustering of conserved residues on the surface of Ral-GppNHp identifies two putative sites for protein-protein interaction, one of which is adjacent to switch I and the other is modulated by switch II and is obstructed in RAl-GDP. (via Semantic Scholar)
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8. Decent Work and Economic Growth (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

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