Crystallization and initial crystal characterization of the N-terminal DH/PH domain of Trio

被引：2
|
作者：
Skowronek, K
Ghumman, M
Zheng, Y
Nassar, N [1 ]
机构：
[1] SUNY Stony Brook, Dept Physiol & Biophys, Stony Brook, NY 11794 USA
[2] Childrens Hosp Res Fdn, Div Expt Hematol, Cincinnati, OH 45229 USA
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2003年 / 59卷
关键词：
D O I：
10.1107/S0907444903009442
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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)2(1), with one TrioN molecule in the asymmetric unit and diffracts to 1.7 Angstrom resolution. The unit-cell parameters are a=b=99.5, c=98.3 Angstrom, alpha=beta=90, gamma=120degrees. A greater than 90% complete native data set has been collected and structure determination using the multiple isomorphous replacement (MIR) method is ongoing.
引用
收藏
页码：1273 / 1275
页数：3
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