5irc | pdb_00005irc

p190A GAP domain complex with RhoA

spinqualitylabelsall models 5irc, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5irc is a 4 chain structure with sequence from Homo sapiens and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.72Å Ligands: CL, CSX, GDP, MG, MGF Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RHG35_RAT Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'. May transduce signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP). May also act as a tumor suppressor (By similarity). Publication Abstract from PubMed Rho GTPase-activating proteins (RhoGAPs) are one of the major classes of regulators of the Rho-related protein family that are crucial in many cellular processes, motility, contractility, growth, differentiation, and development. Using database searches we extracted 66 distinct human RhoGAPs, from which 57 have got a common catalytic domain capable of terminating Rho protein signaling by stimulating the slow intrinsic GTP hydrolysis (GTPase) reaction. The specificity of the majority of the members of RhoGAP family is largely uncharacterized. Here, we comprehensively investigated the sequence-structure-function relationship between RhoGAPs and Rho proteins by combining our in vitro data with in silico data. The activity of 14 representatives of the RhoGAP family towards 12 Rho family proteins was determined in real-time. We identified and structurally verified hotspots in the interface between RhoGAPs and Rho proteins as critical determinants for binding and catalysis. We have found that the RhoGAP domain itself is nonselective and in some cases rather inefficient under cell-free conditions. Thus, we propose that other domains of RhoGAPs confer substrate specificity and fine-tune their catalytic efficiency in cells. Deciphering the molecular and functional basis of RhoGAP family proteins: A systematic approach towards selective inactivation of Rho family proteins.,Amin E, Jaiswal M, Derewenda U, Reis K, Nouri K, Koessmeier KT, Aspenstrom P, Somlyo AV, Dvorsky R, Ahmadian MR J Biol Chem. 2016 Aug 1. pii: jbc.M116.736967. PMID:27481945 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Rho GTPase 3D structures Rho GTPase activating protein 3D structures

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