3BL8

Crystal structure of the extracellular domain of neuroligin 2A from mouse

3BL8 の概要

• エントリーDOI: 10.2210/pdb3bl8/pdb
• 分子名称: Neuroligin-2, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: neuroligin 2a, cell adhesion, glycoprotein, membrane, phosphoprotein, transmembrane
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 261667.27

構造登録者

Jin, X.,Koehnke, J.,Shapiro, L. (登録日: 2007-12-10, 公開日: 2008-02-19, 最終更新日: 2024-10-30)

主引用文献

Koehnke, J.,Jin, X.,Budreck, E.C.,Posy, S.,Scheiffele, P.,Honig, B.,Shapiro, L.
Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2.
Proc.Natl.Acad.Sci.Usa, 105:1873-1878, 2008

PubMed Abstract: Neuroligins (NLs) are catalytically inactive members of a family of cholinesterase-like transmembrane proteins that mediate cell adhesion at neuronal synapses. Postsynaptic neuroligins engage in Ca2+-dependent transsynaptic interactions via their extracellular cholinesterase domain with presynaptic neurexins (NRXs). These interactions may be regulated by two short splice insertions (termed A and B) in the NL cholinesterase domain. Here, we present the 3.3-A crystal structure of the ectodomain from NL2 containing splice insertion A (NL2A). The overall structure of NL2A resembles that of cholinesterases, but several structural features are unique to the NL proteins. First, structural elements surrounding the esterase active-site region differ significantly between active esterases and NL2A. On the opposite surface of the NL2A molecule, the positions of the A and B splice insertions identify a candidate NRX interaction site of the NL protein. Finally, sequence comparisons of NL isoforms allow for mapping the location of residues of previously identified mutations in NL3 and NL4 found in patients with autism spectrum disorders. Overall, the NL2 structure promises to provide a valuable model for dissecting NL isoform- and synapse-specific functions.

PubMed: 18250328
DOI: 10.1073/pnas.0711701105

実験手法

X-RAY DIFFRACTION (3.3 Å)