3R0N

Crystal Structure of the Immunoglobulin variable domain of Nectin-2

3R0N の概要

• エントリーDOI: 10.2210/pdb3r0n/pdb
• 分子名称: Poliovirus receptor-related protein 2, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: ig-domain, cell-adhesion molecule, virus entry receptor, structural genomics, psi-biology, new york structural genomics research consortium, nysgrc, cell adhesion, atoms-to-animals: the immune function network, ifn
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein: Q92692
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14010.54

構造登録者

Ramagopal, U.A.,Samanta, D.,Nathenson, S.G.,Almo, S.C.,New York Structural Genomics Research Consortium (NYSGRC),Atoms-to-Animals: The Immune Function Network (IFN) (登録日: 2011-03-08, 公開日: 2011-04-27, 最終更新日: 2024-11-20)

主引用文献

Samanta, D.,Ramagopal, U.A.,Rubinstein, R.,Vigdorovich, V.,Nathenson, S.G.,Almo, S.C.
Structure of Nectin-2 reveals determinants of homophilic and heterophilic interactions that control cell-cell adhesion.
Proc.Natl.Acad.Sci.USA, 109:14836-14840, 2012

PubMed Abstract: Nectins are members of the Ig superfamily that mediate cell-cell adhesion through homophilic and heterophilic interactions. We have determined the crystal structure of the nectin-2 homodimer at 1.3 Å resolution. Structural analysis and complementary mutagenesis studies reveal the basis for recognition and selectivity among the nectin family members. Notably, the close proximity of charged residues at the dimer interface is a major determinant of the binding affinities associated with homophilic and heterophilic interactions within the nectin family. Our structural and biochemical data provide a mechanistic basis to explain stronger heterophilic versus weaker homophilic interactions among these family members and also offer insights into nectin-mediated transinteractions between engaging cells.

PubMed: 22927415
DOI: 10.1073/pnas.1212912109

実験手法

X-RAY DIFFRACTION (1.3 Å)