4JHR

An auto-inhibited conformation of LGN reveals a distinct interaction mode between GoLoco motifs and TPR motifs

Summary for 4JHR

• Entry DOI: 10.2210/pdb4jhr/pdb
• Descriptor: G-protein-signaling modulator 2 (1 entity in total)
• Functional Keywords: tpr motifs, goloco tandem motifs, asymmetric cell division, lgn, goloco, signaling protein
• Biological source: Mus musculus (mouse); More
• Cellular location: Cytoplasm : Q8VDU0
• Total number of polymer chains: 2
• Total formula weight: 73758.41

Authors

Pan, Z.,Zhu, J.,Shang, Y.,Wei, Z.,Jia, M.,Xia, C.,Wen, W.,Wang, W.,Zhang, M. (deposition date: 2013-03-05, release date: 2013-06-05, Last modification date: 2024-10-30)

Primary citation

Pan, Z.,Zhu, J.,Shang, Y.,Wei, Z.,Jia, M.,Xia, C.,Wen, W.,Wang, W.,Zhang, M.
An autoinhibited conformation of LGN reveals a distinct interaction mode between GoLoco motifs and TPR motifs
Structure, 21:1007-1017, 2013

PubMed Abstract: LGN plays essential roles in asymmetric cell divisions via its N-terminal TPR-motif-mediated binding to mInsc and NuMA. This scaffolding activity requires the release of the autoinhibited conformation of LGN by binding of Gα(i) to its C-terminal GoLoco (GL) motifs. The interaction between the GL and TPR motifs of LGN represents a distinct GL/target binding mode with an unknown mechanism. Here, we show that two consecutive GL motifs of LGN form a minimal TPR-motif-binding unit. GL12 and GL34 bind to TPR0-3 and TPR4-7, respectively. The crystal structure of a truncated LGN reveals that GL34 forms a pair of parallel α helices and binds to the concave surface of TPR4-7, thereby preventing LGN from binding to other targets. Importantly, the GLs bind to TPR motifs with a mode distinct from that observed in the GL/Gα(i)·GDP complexes. Our results also indicate that multiple and orphan GL motif proteins likely respond to G proteins with distinct mechanisms.

PubMed: 23665171
DOI: 10.1016/j.str.2013.04.005

Experimental method

X-RAY DIFFRACTION (2.8 Å)