3MVS

Structure of the N-terminus of Cadherin 23

3MVS の概要

• エントリーDOI: 10.2210/pdb3mvs/pdb
• 分子名称: Cadherin-23, CALCIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: cadherin, adhesion, extracellular domain, 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 (By similarity): Q99PF4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24880.75

構造登録者

Clark, P.,Joseph, J.S.,Kolatkar, A.R. (登録日: 2010-05-04, 公開日: 2010-06-09, 最終更新日: 2024-02-21)

主引用文献

Elledge, H.M.,Kazmierczak, P.,Clark, P.,Joseph, J.S.,Kolatkar, A.,Kuhn, P.,Muller, U.
Structure of the N terminus of cadherin 23 reveals a new adhesion mechanism for a subset of cadherin superfamily members.
Proc.Natl.Acad.Sci.USA, 107:10708-10712, 2010

PubMed Abstract: The cadherin superfamily encodes more than 100 receptors with diverse functions in tissue development and homeostasis. Classical cadherins mediate adhesion by binding interactions that depend on their N-terminal extracellular cadherin (EC) domains, which swap N-terminal beta-strands. Sequence alignments suggest that the strand-swap binding mode is not commonly used by functionally divergent cadherins. Here, we have determined the structure of the EC1-EC2 domains of cadherin 23 (CDH23), which binds to protocadherin 15 (PCDH15) to form tip links of mechanosensory hair cells. Unlike classical cadherins, the CDH23 N terminus contains polar amino acids that bind Ca(2+). The N terminus of PCDH15 also contains polar amino acids. Mutations in polar amino acids within EC1 of CDH23 and PCDH15 abolish interaction between the two cadherins. PCDH21 and PCDH24 contain similarly charged N termini, suggesting that a subset of cadherins share a common interaction mechanism that differs from the strand-swap binding mode of classical cadherins.

PubMed: 20498078
DOI: 10.1073/pnas.1006284107

実験手法

X-RAY DIFFRACTION (1.1 Å)