1P2T

H-Ras 166 in Aqueous mother liqour, RT

Summary for 1P2T

• Entry DOI: 10.2210/pdb1p2t/pdb
• Related: 1P2S 1P2U 1P2V
• Descriptor: Transforming protein p21/H-RAS-1, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total)
• Functional Keywords: molecular switch protein, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Lipid-anchor; Cytoplasmic side: P01112
• Total number of polymer chains: 1
• Total formula weight: 19421.69

Authors

Buhrman, G.K.,de Serrano, V.,Mattos, C. (deposition date: 2003-04-16, release date: 2003-08-05, Last modification date: 2023-08-16)

Primary citation

Buhrman, G.K.,de Serrano, V.,Mattos, C.
Organic solvents order the dynamic switch II in Ras crystals
Structure, 11:747-751, 2003

PubMed Abstract: Room temperature crystal structures of crosslinked H-Ras bound to GMPPNP were solved in 50% 2,2,2-trifluoroethanol, 60% 1,6-hexanediol, and 50% isopropanol. The disordered switch II region of Ras is ordered in the presence of 2,2,2-trifluoroethanol or 1,6-hexanediol. The overall backbone conformation of switch II in these organic solvents is the same as in the Ras-GMPPNP complexes with RalGDS, PI(3) kinase, and RasGAP, indicating a biologically relevant form. Key polar interactions that stabilize the ordered switch are enhanced in the presence of hydrophobic cosolvents. These results suggest that hydrophobic solvents can be used in general to order short biologically relevant segments of disordered regions in protein crystals by favoring H-bonding interactions between atoms that are highly solvated and mobile in aqueous solution.

PubMed: 12842038
DOI: 10.1016/S0969-2126(03)00128-X

Experimental method

X-RAY DIFFRACTION (2 Å)