Structure of nectin-2 reveals determinants of homophilic and heterophilic interactions that control cell-cell adhesion

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 37, 2012, Pages 14836-14840

  Samanta, Dibyendu ^a   Ramagopal, Udupi A ^a,b   Rubinstein, Rotem ^a   Vigdorovich, Vladimir ^a   Nathenson, Stanley G ^a   Almo, Steven C ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b POORNAPRAJNA INSTITUTE OF SCIENTIFIC RESEARCH   (India)

Author keywords

Cell adhesion molecule; Immunoglobulin superfamily; Nectin 2 dimer; X ray crystallography

Indexed keywords

HOMODIMER; NECTIN 1; NECTIN 2;

ARTICLE; BINDING AFFINITY; CELL ADHESION; CONTROLLED STUDY; CRYSTAL STRUCTURE; IMMUNOGLOBULIN VARIABLE REGION; MOLECULAR MODEL; MOLECULAR WEIGHT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; STRUCTURE ANALYSIS;

BASE SEQUENCE; CELL ADHESION; CELL ADHESION MOLECULES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PROTEIN BINDING; PROTEIN INTERACTION MAPS; SEQUENCE ANALYSIS, DNA;

EID: 84866274323     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1212912109     Document Type: Article

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