caa a22 4500 606176594 CHVBK 20210128100748.0 cr unu---uuuuu 210128e20150201xx s 000 0 eng 10.1007/s00018-014-1763-4 doi (NATIONALLICENCE)springer-10.1007/s00018-014-1763-4 Nectin family of cell-adhesion molecules: structural and molecular aspects of function and specificity [Elektronische Daten] [Dibyendu Samanta, Steven Almo] Cell-cell adhesive processes are central to the physiology of multicellular organisms. A number of cell surface molecules contribute to cell-cell adhesion, and the dysfunction of adhesive processes underlies numerous developmental defects and inherited diseases. The nectins, a family of four immunoglobulin superfamily members (nectin-1 to -4), interact through their extracellular domains to support cell-cell adhesion. While both homophilic and heterophilic interactions among the nectins are implicated in cell-cell adhesion, cell-based and biochemical studies suggest heterophilic interactions are stronger than homophilic interactions and control a range of physiological processes. In addition to interactions within the nectin family, heterophilic associations with nectin-like molecules, immune receptors, and viral glycoproteins support a wide range of biological functions, including immune modulation, cancer progression, host-pathogen interactions and immune evasion. We review current structural and molecular knowledge of nectin recognition processes, with a focus on the biochemical and biophysical determinants of affinity and selectivity that drive distinct nectin associations. These proteins and interactions are discussed as potential targets for immunotherapy. Springer Basel, 2014 Nectin nationallicence Nectin-like molecules nationallicence Immunoglobulin fold nationallicence Crystal structures nationallicence Nectin homodimers nationallicence Cadherin nationallicence Immune receptors nationallicence Viral entry receptors nationallicence Samanta Dibyendu Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave, 10461, Bronx, NY, USA aut Almo Steven Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave, 10461, Bronx, NY, USA aut Cellular and Molecular Life Sciences Springer Basel 72/4(2015-02-01), 645-658 1420-682X 72:4<645 2015 72 18 https://doi.org/10.1007/s00018-014-1763-4 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00018-014-1763-4 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Samanta Dibyendu Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave, 10461, Bronx, NY, USA aut NATIONALLICENCE 700 1- Almo Steven Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave, 10461, Bronx, NY, USA aut NATIONALLICENCE 773 0- Cellular and Molecular Life Sciences Springer Basel 72/4(2015-02-01), 645-658 1420-682X 72:4<645 2015 72 18