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1NCJ

N-CADHERIN, TWO-DOMAIN FRAGMENT

1NCJ の概要
エントリーDOI10.2210/pdb1ncj/pdb
分子名称PROTEIN (N-CADHERIN), CALCIUM ION, URANYL (VI) ION (3 entities in total)
機能のキーワードcell adhesion protein
由来する生物種Mus musculus (house mouse)
細胞内の位置Cell membrane; Single-pass type I membrane protein: P15116
タンパク質・核酸の鎖数1
化学式量合計23993.73
構造登録者
Tamura, K.,Shan, W.-S.,Hendrickson, W.A.,Colman, D.R.,Shapiro, L. (登録日: 1999-02-02, 公開日: 1999-03-18, 最終更新日: 2023-08-16)
主引用文献Tamura, K.,Shan, W.S.,Hendrickson, W.A.,Colman, D.R.,Shapiro, L.
Structure-function analysis of cell adhesion by neural (N-) cadherin.
Neuron, 20:1153-1163, 1998
Cited by
PubMed Abstract: To investigate the possible biological function of the lateral "strand dimer" observed in crystal structures of a D1 domain extracellular fragment from N-cadherin, we have undertaken site-directed mutagenesis studies of this molecule. Mutation of most residues important in the strand dimer interface abolish the ability of N-cadherin to mediate cell adhesion. Mutation of an analogous central residue (Trp-2) in E-cadherin also abrogates the adhesive capacity of that molecule. We also determined the crystal structure of a Ca2+-complexed two-domain fragment from N-cadherin. This structure, like its E-cadherin counterpart, does not adopt the strand dimer conformation. This suggests the possibility that classical cadherins might stably exist in both dimeric and monomeric forms. Data from several laboratories imply that lateral dimerization or clustering of cadherins may increase their adhesivity. We suggest the possibility that the strand dimer may play a role in this activation.
PubMed: 9655503
DOI: 10.1016/S0896-6273(00)80496-1
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.4 Å)
構造検証レポート
Validation report summary of 1ncj
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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