1hh4

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1hh4, resolution 2.7Å

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RAC1-RHOGDI COMPLEX INVOLVED IN NADPH OXIDASE ACTIVATION

Overview

A heterodimer of prenylated Rac1 and Rho GDP dissociation inhibitor was, purified and found to be competent in NADPH oxidase activation. Small, angle neutron scattering experiments confirmed a 1:1 stoichiometry. The, crystal structure of the Rac1-RhoGDI complex was determined at 2.7 A, resolution. In this complex in which Rac1 is bound to GDP, the switch I, region of Rac1 is in the GDP conformation whereas the switch II region, resembles that of a GTP-bound GTPase. Two types of interaction between, RhoGTPases and RhoGDI were investigated. The lipid-protein interaction, between the geranylgeranyl moiety of Rac1 and RhoGDI resulted in numerous, structural changes in the core of RhoGDI. The interactions between Rac1, and RhoGDI occur through hydrogen bonds which involve a number of residues, ... [(full description)]

About this Structure

1HH4 is a [Protein complex] structure of sequences from [Homo sapiens] with MG, GDP and GER as [ligands]. Full crystallographic information is available from [OCA].

Reference

Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation., Grizot S, Faure J, Fieschi F, Vignais PV, Dagher MC, Pebay-Peyroula E, Biochemistry. 2001 Aug 28;40(34):10007-13. PMID:11513578

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