3TVD

Crystal Structure of Mouse RhoA-GTP complex

Summary for 3TVD

• Entry DOI: 10.2210/pdb3tvd/pdb
• Related: 1A2B 1CC0 1FTN
• Descriptor: Transforming protein RhoA, 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: alpha helical, protein_gtp complex, helical protein, gtp binding protein, regulates signal transduction pathway, gtp, nil, membrane, signaling protein
• Biological source: Rattus norvegicus (rat)
• Cellular location: Cell membrane; Lipid-anchor; Cytoplasmic side (By similarity): P61589
• Total number of polymer chains: 2
• Total formula weight: 44753.47

Authors

Swaminathan, K.,Pal, K.,Jobichen, C. (deposition date: 2011-09-20, release date: 2012-10-10, Last modification date: 2023-11-01)

Primary citation

Jobichen, C.,Pal, K.,Swaminathan, K.
Crystal structure of mouse RhoA:GTPgammaS complex in a centered lattice.
J.Struct.Funct.Genom., 13:241-245, 2012

PubMed Abstract: RhoA, 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.

PubMed: 23001747
DOI: 10.1007/s10969-012-9143-5

Experimental method

X-RAY DIFFRACTION (2.989 Å)