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Crystal structure of mouse RhoA:GTPγS complex in a centered lattice

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Journal of Structural and Functional Genomics

Abstract

RhoA, a member of the Rho sub-family of small GTPases, plays a significant signaling role in cell morphogenesis, migration, neuronal development, cell division and adhesion. So far, 4 structures of RhoA:GDP/GTP analogs and 14 structures of RhoA in complex with other proteins have been reported. All RhoA:GDP/GTP analog complexes have been crystallized in primitive lattices and RhoA is monomeric. This is the first time a RhoA:GTP analog complex has been crystallized as a dimer in a centered lattice. The present structure reveals structural differences in the switch-I (residues 28–42) and switch-II (residues 61–66) regions, which play important roles in interactions with downstream targets to transduce signals, when compared to the previously reported structures.

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Acknowledgments

This project was supported by a grant from Ministry of Education, Singapore to KS. The graduate scholarship for KP was provided by National University of Singapore and CJ is supported by a Life Science Institute grant. The project was conceived by KS, the complex was crystallized by KP and CJ collected data and solved the structure. All three authors prepared the manuscript. The authors declare no financial interest.

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Authors and Affiliations

  1. Department of Biological Sciences, National University of Singapore, Singapore, 117543, Singapore

    Chacko Jobichen, Kuntal Pal & Kunchithapadam Swaminathan

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  1. Chacko Jobichen
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  2. Kuntal Pal
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  3. Kunchithapadam Swaminathan
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Corresponding author

Correspondence to Kunchithapadam Swaminathan.

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Chacko Jobichen and Kuntal Pal are contributed equally.

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Jobichen, C., Pal, K. & Swaminathan, K. Crystal structure of mouse RhoA:GTPγS complex in a centered lattice. J Struct Funct Genomics 13, 241–245 (2012). https://doi.org/10.1007/s10969-012-9143-5

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  • DOI: https://doi.org/10.1007/s10969-012-9143-5

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