Crystallization and initial crystal characterization of the N-terminal DH/PH domain of Trio.
Trio is a multidomain signaling protein that plays an important role in neurite outgrowth, axon guidance and skeletal muscle development. Trio contains two DH/PH tandem domains that respectively activate the small GTPases RhoG/Rac and RhoA. The N-terminal DH/PH domain, TrioN, crystallizes in space group P3(1)21, with one TrioN molecule in the asymmetric unit and diffracts to 1.7 A resolution. The unit-cell parameters are a = b = 99.5, c = 98.3 A, alpha = beta = 90, gamma = 120 degrees. A greater than 90% complete native data set has been collected and structure determination using the multiple isomorphous replacement (MIR) method is ongoing.
Skowronek
Karlheinz
K
Department of Physiology and Biophysics, Stony Brook University, Stony Brook, NY 11794-8661, USA.
Ghumman
Mohammed
M
Zheng
Yi
Y
Nassar
Nicolas
N
D003460:Crystallization / Q000379:methods; D020662:Guanine Nucleotide Exchange Factors; D006801:Humans; D010750:Phosphoproteins / Q000737:chemistry* / Q000302:isolation & purification; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry* / Q000302:isolation & purification; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction / Q000379:methods
D020662:Guanine Nucleotide Exchange Factors; D010750:Phosphoproteins; D017346:Protein Serine-Threonine Kinases; C099628:TRIO protein, human