Motion in G(i alpha 1) [gia1]

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Classification Known Domain Motion, Partial Refolding of Structure [D-f-2]

Structures 1GDD Conformation 1 [ PartsList ]

Description Twenty-five residues from Asp9 to Glu33 along with eleven COOH-terminal residues fold into a compact microdomain at the NH2-terminal edge of the Ras domain beta sheet in one complex ( G(i alpha 1)-GDP (PDB id 1GDD) ) as compared with the another (the -GTPgS complex), although the overall canonical Ras-like alpha-beta fold is preserved in both conformations.

Particular values describing motion Maximum CA displacement (A) = 2.1 (Greater than 2 angstroms.) Experimental Methods = x (Traditional x-ray) Creation Date = 19971130 Modification Date = 19971212

References M B Mixon, E Lee, D E Coleman, A M Berghuis, A G Gilman, S R Sprang (1995). Tertiary and Quarternary Structural Changes in G(i alpha 1) Induced by GTP Hydrolysis. Sci. 270:954-960. [Medline info for 95050585] H R Bourne (1995). Trimeric G Proteins: Surprise Witness Tells a Tale. Sci. 270:933-934. [Medline info for 95050585]

GO terms associated with structures Molecular function signal transducer activity, GTP binding Biological process signal transduction, G-protein coupled receptor protein signaling pathway

Morphs

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Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu