3X1Z

Ras-related protein Rap1B(T65A) with GppNHp

Summary for 3X1Z

• Entry DOI: 10.2210/pdb3x1z/pdb
• Related: 3W1W 3W1X 3W1Y
• Descriptor: Ras-related protein Rap-1b, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: signal transduction, signaling protein
• Biological source: Rattus norvegicus (brown rat,rat,rats)
• Cellular location: Cell membrane : Q62636
• Total number of polymer chains: 2
• Total formula weight: 39112.01

Authors

Noguchi, H.,Ikegami, T.,Park, S.Y.,Tame, J.R.H.,Unzai, S. (deposition date: 2014-12-02, release date: 2015-06-03, Last modification date: 2024-03-20)

Primary citation

Noguchi, H.,Ikegami, T.,Nagadoi, A.,Kamatari, Y.O.,Park, S.Y.,Tame, J.R.,Unzai, S.
The structure and conformational switching of Rap1B
Biochem.Biophys.Res.Commun., 462:46-51, 2015

PubMed Abstract: Rap1B is a small GTPase involved in the regulation of numerous cellular processes including synaptic plasticity, one of the bases of memory. Like other members of the Ras family, the active GTP-bound form of Rap1B can bind to a large number of effector proteins and so transmit signals to downstream components of the signaling pathways. The structure of Rap1B bound only to a nucleotide has yet to be solved, but might help reveal an inactive conformation that can be stabilized by a small molecule drug. Unlike other Ras family proteins such as H-Ras and Rap2A, Rap1B crystallizes in an intermediate state when bound to a non-hydrolyzable GTP analog. Comparison with H-Ras and Rap2A reveals conservative mutations relative to Rap1B, distant from the bound nucleotide, which control how readily the protein may adopt the fully activated form in the presence of GTP. High resolution crystallographic structures of mutant proteins show how these changes may influence the hydrogen bonding patterns of the key switch residues.

PubMed: 25935485
DOI: 10.1016/j.bbrc.2015.04.103

Experimental method

X-RAY DIFFRACTION (1.25 Å)