1FTN

CRYSTAL STRUCTURE OF THE HUMAN RHOA/GDP COMPLEX

Summary for 1FTN

• Entry DOI: 10.2210/pdb1ftn/pdb
• Descriptor: TRANSFORMING PROTEIN RHOA (H12), MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: proto-oncogene, gtp-binding, prenylation, lipoprotein, small p-protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Lipid-anchor; Cytoplasmic side: P61586
• Total number of polymer chains: 1
• Total formula weight: 22233.59

Authors

Wei, Y.,Zhang, Y.,Derewenda, U.,Liu, X.,Minor, W.,Nakamoto, R.K.,Somlyo, A.V.,Somlyo, A.P.,Derewenda, Z.S. (deposition date: 1997-03-13, release date: 1998-03-18, Last modification date: 2024-04-03)

Primary citation

Wei, Y.,Zhang, Y.,Derewenda, U.,Liu, X.,Minor, W.,Nakamoto, R.K.,Somlyo, A.V.,Somlyo, A.P.,Derewenda, Z.S.
Crystal structure of RhoA-GDP and its functional implications.
Nat.Struct.Biol., 4:699-703, 1997

PubMed Abstract: RhoA, a ubiquitous intracellular GTPase, mediates cytoskeletal responses to extracellular signals. A 2.1 A resolution crystal structure of the human RhoA-GDP complex shows unique stereochemistry in the switch I region, which results in a novel mode of Mg2+ binding.

PubMed: 9302995
DOI: 10.1038/nsb0997-699

Experimental method

X-RAY DIFFRACTION (2.1 Å)