3TAD

Crystal Structure of the Liprin-alpha/Liprin-beta complex

Summary for 3TAD

• Entry DOI: 10.2210/pdb3tad/pdb
• Related: 3TAC
• Descriptor: Liprin-alpha-2, Liprin-beta-1, GLYCEROL, ... (4 entities in total)
• Functional Keywords: protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: O75334
• Total number of polymer chains: 4
• Total formula weight: 129774.11

Authors

Wei, Z.,Zheng, S.,Yu, C.,Zhang, M. (deposition date: 2011-08-04, release date: 2011-10-12, Last modification date: 2024-03-20)

Primary citation

Wei, Z.,Zheng, S.,Spangler, S.A.,Yu, C.,Hoogenraad, C.C.,Zhang, M.
Liprin-mediated large signaling complex organization revealed by the liprin-alpha/CASK and liprin-alpha/liprin-beta complex structures
Mol.Cell, 43:586-598, 2011

PubMed Abstract: Liprins are highly conserved scaffold proteins that regulate cell adhesion, cell migration, and synapse development by binding to diverse target proteins. The molecular basis governing liprin/target interactions is poorly understood. The liprin-α2/CASK complex structure solved here reveals that the three SAM domains of liprin-α form an integrated supramodule that binds to the CASK kinase-like domain. As supported by biochemical and cellular studies, the interaction between liprin-α and CASK is unique to vertebrates, implying that the liprin-α/CASK interaction is likely to regulate higher-order brain functions in mammals. Consistently, we demonstrate that three recently identified X-linked mental retardation mutants of CASK are defective in binding to liprin-α. We also solved the liprin-α/liprin-β SAM domain complex structure, which uncovers the mechanism underlying liprin heterodimerizaion. Finally, formation of the CASK/liprin-α/liprin-β ternary complex suggests that liprins can mediate assembly of target proteins into large protein complexes capable of regulating numerous cellular activities.

PubMed: 21855798
DOI: 10.1016/j.molcel.2011.07.021

Experimental method

X-RAY DIFFRACTION (2.9 Å)