Sequence and structural determinants of strand swapping in cadherin domains: do all cadherins bind through the same adhesive interface?

ABSTRACT: Cadherins are cell surface adhesion proteins important for tissue development and integrity. Type I and type II, or classical, cadherins form adhesive dimers via an interface formed through the exchange, or "swapping", of the N-terminal beta-strands from their membrane-distal EC1 domains. Here, we ask which sequence and structural features in EC1 domains are responsible for beta-strand swapping and whether members of other cadherin families form similar strand-swapped binding interfaces. We created a comprehensive database of multiple alignments of each type of cadherin domain. We used the known three-dimensional structures of classical cadherins to identify conserved positions in multiple sequence alignments that appear to be crucial determinants of the cadherin domain structure. We ident

SUBMITTER: Posy S 

PROVIDER: S-EPMC2435303 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature