1QZ1

Crystal Structure of the Ig 1-2-3 fragment of NCAM

1QZ1 の概要

• エントリーDOI: 10.2210/pdb1qz1/pdb
• 関連するPDBエントリー: 1EPF 2NCM 3NCM
• 分子名称: Neural cell adhesion molecule 1, 140 kDa isoform (2 entities in total)
• 機能のキーワード: ig modules, cell adhesion, ncam
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein: P13596
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32407.22

構造登録者

Soroka, V.,Kolkova, K.,Kastrup, J.S.,Diederichs, K.,Breed, J.,Kiselyov, V.V.,Poulsen, F.M.,Larsen, I.K.,Welte, W.,Berezin, V.,Bock, E.,Kasper, C. (登録日: 2003-09-15, 公開日: 2003-11-04, 最終更新日: 2024-10-16)

主引用文献

Soroka, V.,Kolkova, K.,Kastrup, J.S.,Diederichs, K.,Breed, J.,Kiselyov, V.V.,Poulsen, F.M.,Larsen, I.K.,Welte, W.,Berezin, V.,Bock, E.,Kasper, C.
Structure and interactions of NCAM Ig1-2-3 suggest a novel zipper mechanism for homophilic adhesion
Structure, 11:1291-1301, 2003

PubMed Abstract: The neural cell adhesion molecule, NCAM, mediates Ca(2+)-independent cell-cell and cell-substratum adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM molecules) binding. NCAM plays a key role in neural development, regeneration, and synaptic plasticity, including learning and memory consolidation. The crystal structure of a fragment comprising the three N-terminal Ig modules of rat NCAM has been determined to 2.0 A resolution. Based on crystallographic data and biological experiments we present a novel model for NCAM homophilic binding. The Ig1 and Ig2 modules mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), whereas the Ig3 module mediates interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through simultaneous binding to the Ig1 and Ig2 modules. This arrangement results in two perpendicular zippers forming a double zipper-like NCAM adhesion complex.

PubMed: 14527396
DOI: 10.1016/j.str.2003.09.006

実験手法

X-RAY DIFFRACTION (2 Å)