1LWR

Solution structure of the NCAM fibronectin type III module 2

1LWR の概要

• エントリーDOI: 10.2210/pdb1lwr/pdb
• 分子名称: Neural Cell Adhesion Molecule 1, 140 kDa isoform (1 entity in total)
• 機能のキーワード: all beta, fibronectin type iii module, cell adhesion
• 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: 10657.96

構造登録者

Kiselyov, V.V.,Skladchikova, G.,Hinsby, A.M.,Jensen, P.H.,Kulahin, N.,Pedersen, N.,Tsetlin, V.,Poulsen, F.M.,Berezin, V.,Bock, E. (登録日: 2002-06-03, 公開日: 2003-06-03, 最終更新日: 2024-05-22)

主引用文献

Kiselyov, V.V.,Skladchikova, G.,Hinsby, A.M.,Jensen, P.H.,Kulahin, N.,Soroka, V.,Pedersen, N.,Tsetlin, V.,Poulsen, F.M.,Berezin, V.,Bock, E.
Structural basis for a direct interaction between FGFR1 and NCAM and evidence for a regulatory role of ATP
Structure, 11:691-701, 2003

PubMed Abstract: The neural cell adhesion molecule (NCAM) promotes axonal outgrowth, presumably through an interaction with the fibroblast growth factor receptor (FGFR). NCAM also has a little-understood ATPase activity. We here demonstrate for the first time a direct interaction between NCAM (fibronectin type III [F3] modules 1 and 2) and FGFR1 (Ig modules 2 and 3) by surface plasmon resonance (SPR) analysis. The structure of the NCAM F3 module 2 was determined by NMR and the module was shown by NMR to interact with the FGFR1 Ig module 3 and ATP. The NCAM sites binding to FGFR and ATP were found to overlap and ATP was shown by SPR to inhibit the NCAM-FGFR binding, indicating that ATP probably regulates the NCAM-FGFR interaction. Furthermore, we demonstrate that the NCAM module was able to induce activation (phosphorylation) of FGFR and to stimulate neurite outgrowth. In contrast, ATP inhibited neurite outgrowth induced by the module.

PubMed: 12791257
DOI: 10.1016/S0969-2126(03)00096-0

実験手法

SOLUTION NMR