C-Cadherin Ectodomain Structure and Implications for Cell Adhesion Mechanisms

By T. Boggon, J. Murray, S. Chappuis-Flament, E. Wong, B. Gumbiner, L. Shapiro. Science, 2002

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Nectin and afadin: novel organizers of intercellular junctions (2003, background): “…and N-cadherin and of the whole domains (EC1-EC5) of C-cadherin (Shapiro et al., 1995; Nagar et al., 1996; Tamura et al., 1998; Pertz et al., 1999; Boggon et al., 2002), cadherin first forms a cis-dimer, in which the monomers are aligned in a parallel orientation, and then a trans-dimer, in which…”
Regulation of cadherin-mediated adhesion in morphogenesis (2005, background): “The extracellular domain of the classic cadherin molecule consists of five cadherin-type repeats, called EC (extracellular cadherin) domains that are bound together by Ca 2+ in a rod-like structur”
Discovery Through the Computational Microscope (2009, neutral): “Structu (Boggon et al., 2002) revealed several known and unknown properties that are likely to hold for all cadherin repeats (Sotomayor and Schulten, 2008).”
Biological Physics of the Developing Embryo (2005, neutral): “Particularly detailed studies have been performed in the case of cadherins (Shapiro et al., 1995; Nagar et al., 1996; Angres et al., 1996; Adams et al., 1998; Boggon et al., 2002).”
Membrane fluctuations mediate lateral interaction between cadherin bonds (2017, background): “The sizes of the individual constituents is estimated from structural considerations to be 19 nm (E-cadherin) [1], 7 nm (Fc fragment) and 2 nm (hexahistidin tag).”