4G5O

Structure of LGN GL4/Galphai3(Q147L) complex

Summary for 4G5O

• Entry DOI: 10.2210/pdb4g5o/pdb
• Related: 4G5Q 4G5R 4G5S
• Descriptor: Guanine nucleotide-binding protein G(k) subunit alpha, G-protein-signaling modulator 2, GUANOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: galphai, goloco, galpha signaling, asymmetric cell division, cell cycle-signaling protein complex, cell cycle/signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P08754; Cytoplasm (By similarity): Q8VDU0
• Total number of polymer chains: 8
• Total formula weight: 168585.12

Authors

Jia, M.,Li, J.,Zhu, J.,Wen, W.,Zhang, M.,Wang, W. (deposition date: 2012-07-18, release date: 2012-09-05, Last modification date: 2025-03-05)

Primary citation

Jia, M.,Li, J.,Zhu, J.,Wen, W.,Zhang, M.,Wang, W.
Crystal structures of the scaffolding protein LGN reveal the general mechanism by which GoLoco binding motifs inhibit the release of GDP from G alpha i.
J.Biol.Chem., 287:36766-36776, 2012

PubMed Abstract: GoLoco (GL) motif-containing proteins regulate G protein signaling by binding to Gα subunit and acting as guanine nucleotide dissociation inhibitors. GLs of LGN are also known to bind the GDP form of Gα(i/o) during asymmetric cell division. Here, we show that the C-terminal GL domain of LGN binds four molecules of Gα(i)·GDP. The crystal structures of Gα(i)·GDP in complex with LGN GL3 and GL4, respectively, reveal distinct GL/Gα(i) interaction features when compared with the only high resolution structure known with GL/Gα(i) interaction between RGS14 and Gα(i1.) Only a few residues C-terminal to the conserved GL sequence are required for LGN GLs to bind to Gα(i)·GDP. A highly conserved "double Arg finger" sequence (RΨ(D/E)(D/E)QR) is responsible for LGN GL to bind to GDP bound to Gα(i). Together with the sequence alignment, we suggest that the LGN GL/Gα(i) interaction represents a general binding mode between GL motifs and Gα(i). We also show that LGN GLs are potent guanine nucleotide dissociation inhibitors.

PubMed: 22952234
DOI: 10.1074/jbc.M112.391607

Experimental method

X-RAY DIFFRACTION (2.9 Å)