1CC0

CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX

1CC0 の概要

• エントリーDOI: 10.2210/pdb1cc0/pdb
• 分子名称: transforming protein rhoA, rho GDP dissociation inhibitor alpha, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: rho gtpase, g-protein, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 90292.48

構造登録者

Longenecker, K.L.,Read, P.,Derewenda, U.,Dauter, Z.,Garrard, S.,Walker, L.,Somlyo, A.V.,Somlyo, A.P.,Nakamoto, R.K.,Derewenda, Z.S. (登録日: 1999-03-03, 公開日: 2000-01-07, 最終更新日: 2023-12-27)

主引用文献

Longenecker, K.,Read, P.,Derewenda, U.,Dauter, Z.,Liu, X.,Garrard, S.,Walker, L.,Somlyo, A.V.,Nakamoto, R.K.,Somlyo, A.P.,Derewenda, Z.S.
How RhoGDI binds Rho.
Acta Crystallogr.,Sect.D, 55:1503-1515, 1999

PubMed Abstract: Like all Rho (Ras homology) GTPases, RhoA functions as a molecular switch in cell signaling, alternating between GTP- and GDP-bound states, with its biologically inactive GDP-bound form maintained as a cytosolic complex with RhoGDI (guanine nucleotide-exchange inhibitor). The crystal structures of RhoA-GDP and of the C-terminal immunoglobulin-like domain of RhoGDI (residues 67-203) are known, but the mechanism by which the two proteins interact is not known. The functional human RhoA-RhoGDI complex has been expressed in yeast and crystallized (P6(5)22, unit-cell parameters a = b = 139, c = 253 A, two complexes in the asymmetric unit). Although diffraction from these crystals extends to 3.5 A and is highly anisotropic, the experimentally phased (MAD plus MIR) electron-density map was adequate to reveal the mutual disposition of the two molecules. The result was validated by molecular-replacement calculations when data were corrected for anisotropy. Furthermore, the N-terminus of RhoGDI (the region involved in inhibition of nucleotide exchange) can be identified in the electron-density map: it is bound to the switch I and switch II regions of RhoA, occluding an epitope which binds Dbl-like nucleotide-exchange factors. The entrance of the hydrophobic pocket of RhoGDI is 25 A from the last residue in the RhoA model, with its C-terminus oriented to accommodate the geranylgeranyl group without conformational change in RhoA.

PubMed: 10489445
DOI: 10.1107/S090744499900801X

実験手法

X-RAY DIFFRACTION (5 Å)