3tvd | pdb_00003tvd
From Proteopedia
Crystal Structure of Mouse RhoA-GTP complex
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Structural highlights
Publication Abstract from PubMedRhoA, a member of the Rho sub-family of small GTPases, plays a significant signaling role in cell morphogenesis, migration, neuronal development, cell division and adhesion. So far, 4 structures of RhoA:GDP/GTP analogs and 14 structures of RhoA in complex with other proteins have been reported. All RhoA:GDP/GTP analog complexes have been crystallized in primitive lattices and RhoA is monomeric. This is the first time a RhoA:GTP analog complex has been crystallized as a dimer in a centered lattice. The present structure reveals structural differences in the switch-I (residues 28-42) and switch-II (residues 61-66) regions, which play important roles in interactions with downstream targets to transduce signals, when compared to the previously reported structures. Crystal structure of mouse RhoA:GTPgammaS complex in a centered lattice.,Jobichen C, Pal K, Swaminathan K J Struct Funct Genomics. 2012 Sep 22. PMID:23001747[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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