Ontology highlight
ABSTRACT:
SUBMITTER: Jin X
PROVIDER: S-EPMC3271863 | biostudies-literature | 2012 Jan
REPOSITORIES: biostudies-literature
Jin Xiangshu X Walker Melissa A MA Felsövályi Klára K Vendome Jeremie J Bahna Fabiana F Mannepalli Seetha S Cosmanescu Filip F Ahlsen Goran G Honig Barry B Shapiro Lawrence L
Proceedings of the National Academy of Sciences of the United States of America 20111214 3
Vertebrate classical cadherins mediate selective calcium-dependent cell adhesion by mechanisms now understood at the atomic level. However, structures and adhesion mechanisms of cadherins from invertebrates, which are highly divergent yet function in similar roles, remain unknown. Here we present crystal structures of three- and four-tandem extracellular cadherin (EC) domain segments from Drosophila N-cadherin (DN-cadherin), each including the predicted N-terminal EC1 domain (denoted EC1') of th ...[more]