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1F97

SOLUBLE PART OF THE JUNCTION ADHESION MOLECULE FROM MOUSE

1F97 の概要
エントリーDOI10.2210/pdb1f97/pdb
分子名称JUNCTION ADHESION MOLECULE, MAGNESIUM ION (3 entities in total)
機能のキーワードimmunoglobulin superfamily, beta-sandwich fold, cell adhesion
由来する生物種Mus musculus (house mouse)
細胞内の位置Cell junction, tight junction: O88792
タンパク質・核酸の鎖数1
化学式量合計22875.54
構造登録者
Kostrewa, D.,Brockhaus, M.,D'Arcy, A.,Dale, G.,Bazzoni, G.,Dejana, E.,Winkler, F.,Hennig, M. (登録日: 2000-07-07, 公開日: 2001-01-10, 最終更新日: 2024-11-13)
主引用文献Kostrewa, D.,Brockhaus, M.,D'Arcy, A.,Dale, G.E.,Nelboeck, P.,Schmid, G.,Mueller, F.,Bazzoni, G.,Dejana, E.,Bartfai, T.,Winkler, F.K.,Hennig, M.
X-ray structure of junctional adhesion molecule: structural basis for homophilic adhesion via a novel dimerization motif.
EMBO J., 20:4391-4398, 2001
Cited by
PubMed Abstract: Junctional adhesion molecules (JAMs) are a family of immunoglobulin-like single-span transmembrane molecules that are expressed in endothelial cells, epithelial cells, leukocytes and myocardia. JAM has been suggested to contribute to the adhesive function of tight junctions and to regulate leukocyte trans migration. We describe the crystal structure of the recombinant extracellular part of mouse JAM (rsJAM) at 2.5 A resolution. rsJAM consists of two immunoglobulin-like domains that are connected by a conformationally restrained short linker. Two rsJAM molecules form a U-shaped dimer with highly complementary interactions between the N-terminal domains. Two salt bridges are formed in a complementary manner by a novel dimerization motif, R(V,I,L)E, which is essential for the formation of rsJAM dimers in solution and common to the known members of the JAM family. Based on the crystal packing and studies with mutant rsJAM, we propose a model for homophilic adhesion of JAM. In this model, U-shaped JAM dimers are oriented in cis on the cell surface and form a two-dimensional network by trans-interactions of their N-terminal domains with JAM dimers from an opposite cell surface.
PubMed: 11500366
DOI: 10.1093/emboj/20.16.4391
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 1f97
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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