1H, 13C and 15N resonance assignments of the GTPase-activating (GAP) and Ral binding domains (GBD) of RLIP76 (RalBP1)

被引:4
作者
Rajasekar, Karthik V. [1 ]
Campbell, Louise J. [1 ]
Nietlispach, Daniel [1 ]
Owen, Darerca [1 ]
Mott, Helen R. [1 ]
机构
[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England
基金
英国医学研究理事会; 英国生物技术与生命科学研究理事会;
关键词
RLIP76; RalBP1; Ral GTPase; Multidomain protein; Endocytosis; Signalling; MULTIDIMENSIONAL NMR; PUTATIVE EFFECTOR; PROTEINS; IDENTIFICATION; HOMOLOGY; COMPLEX; TARGET;
D O I
10.1007/s12104-011-9337-y
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
RLIP76 (also known as RalBP1) is an effector for Ral small G proteins. RLIP76 is a multifunctional, multi-domain protein that includes a GTPase activating domain for the Rho family (RhoGAP domain) and a GTPase binding domain (GBD) for the Ral small G proteins. The juxtaposition of these two domains (GAP and GBD) may be a strategy employed to co-ordinate regulation of Rho family and Ral-controlled signalling pathways at a crossover node. Here we present the H-1, N-15 and C-13 NMR backbone and sidechain resonance assignments of the GAP and GBD di-domain (31 kDa).
引用
收藏
页码:119 / 122
页数:4
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