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4NUQ

Crystal structure of mouse N-cadherin EC1-2 W2F

4NUQ の概要
エントリーDOI10.2210/pdb4nuq/pdb
関連するPDBエントリー4NUM 4NUP
分子名称Cadherin-2, CALCIUM ION (3 entities in total)
機能のキーワードcell adhesion molecule, cell adhesion
由来する生物種Mus musculus (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23698.69
構造登録者
Jin, X. (登録日: 2013-12-03, 公開日: 2014-09-24, 最終更新日: 2024-02-28)
主引用文献Vendome, J.,Felsovalyi, K.,Song, H.,Yang, Z.,Jin, X.,Brasch, J.,Harrison, O.J.,Ahlsen, G.,Bahna, F.,Kaczynska, A.,Katsamba, P.S.,Edmond, D.,Hubbell, W.L.,Shapiro, L.,Honig, B.
Structural and energetic determinants of adhesive binding specificity in type I cadherins.
Proc.Natl.Acad.Sci.USA, 111:E4175-E4184, 2014
Cited by
PubMed Abstract: Type I cadherin cell-adhesion proteins are similar in sequence and structure and yet are different enough to mediate highly specific cell-cell recognition phenomena. It has previously been shown that small differences in the homophilic and heterophilic binding affinities of different type I family members can account for the differential cell-sorting behavior. Here we use a combination of X-ray crystallography, analytical ultracentrifugation, surface plasmon resonance and double electron-electron resonance (DEER) electron paramagnetic resonance spectroscopy to identify the molecular determinants of type I cadherin dimerization affinities. Small changes in sequence are found to produce subtle structural and dynamical changes that impact relative affinities, in part via electrostatic and hydrophobic interactions, and in part through entropic effects because of increased conformational heterogeneity in the bound states as revealed by DEER distance mapping in the dimers. These findings highlight the remarkable ability of evolution to exploit a wide range of molecular properties to produce closely related members of the same protein family that have affinity differences finely tuned to mediate their biological roles.
PubMed: 25253890
DOI: 10.1073/pnas.1416737111
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.116 Å)
構造検証レポート
Validation report summary of 4nuq
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2025-12-31に公開中

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