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Ras Superfamily Small G Proteins: Biology and Mechanisms 1 pp 25–50Cite as

The Structure of the G Domain of the Ras Superfamily

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Abstract

Since the first three-dimensional structure of H-Ras has been determined in 1990, the number of solved structures of small GTP-binding proteins has increased tremendously. As of February 2014, 555 structures of Ras-superfamily proteins have been deposited in the protein databank (PDB), either in uncomplexed form or bound to effectors or other regulatory proteins. The 751 chains contain either GTP or a GTP analogue (431 chains) and GDP (320 chains), respectively. This chapter summarizes the most important structural features of single-domain GTP-binding proteins of the Ras superfamily and focuses on the comparison of the solved structures, especially the switch loops, i.e., the regions that change conformation upon nucleotide exchange from GTP to GDP. In particular, the pitfalls of the crystal structure interpretation will be emphasized since flexible protein segments like the switch regions of the G domain are especially prone to crystallization artifacts. Regions that are mobile in solution are commonly “frozen out” into relatively arbitrary conformations that often are dictated by the specifics of the packing against neighboring molecules in the crystals. It requires very careful analysis to decide if the conformations populated in the crystals have any physiological relevance.

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  1. Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Str. 11, 44227, Dortmund, Germany

    Ingrid R. Vetter

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Correspondence to Ingrid R. Vetter .

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  1. Max-Planck-Institute of Molecular Physiology, Dortmund, Nordrhein-Westfalen, Germany

    Alfred Wittinghofer

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Vetter, I.R. (2014). The Structure of the G Domain of the Ras Superfamily. In: Wittinghofer, A. (eds) Ras Superfamily Small G Proteins: Biology and Mechanisms 1. Springer, Vienna. https://doi.org/10.1007/978-3-7091-1806-1_2

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