Structure and Function of Cadherin Extracellular Regions
Cell-surface glycoproteins of the cadherin superfamily are defined by the presence of extracellular cadherin (EC) β-sandwich domains in their extracellular regions. EC domains adopt a fold similar to immunoglobulin domains, but most EC domains ligate calcium through stereotyped sites positioned between successive domains; Ca2+-binding at these sites rigidifies cadherin extracellular regions. Although the superfamily is highly diverse and may serve numerous functions, the best-characterized members are the vertebrate “classical” cadherins, which mediate cell–cell adhesion via homodimerization between their membrane-distal EC1 domains. Nonclassical and invertebrate cadherins have evolved distinct mechanisms for cell recognition and adhesion, and are only now beginning to be understood.
KeywordsCadherin Classical cadherin Extracellular cell adhesion Crystal structure crystallography Cell adhesion Adherens junctions
- Jin X, Walker MA, Felsovalyi K, Vendome J, Bahna F, Mannepalli S, Cosmanescu F, Ahlsen G, Honig B, Shapiro L (2012) Crystal structures of Drosophila N-cadherin ectodomain regions reveal a widely used class of Ca2+-free interdomain linkers. Proc Natl Acad Sci U S A 109:E127–E134CrossRefPubMedPubMedCentralGoogle Scholar
- Morishita H, Umitsu M, Murata Y, Shibata N, Udaka K, Higuchi Y, Akutsu H, Yamaguchi T, Yagi T, Ikegami T (2006) Structure of the cadherin-related neuronal receptor/protocadherin-alpha first extracellular cadherin domain reveals diversity across cadherin families. J Biol Chem 281:33650–33663CrossRefPubMedGoogle Scholar
- Sivasankar S, Zhang Y, Nelson WJ, Chu S (2009) Characterizing the initial encounter complex in cadherin adhesion. Structure 17:1075–1081Google Scholar