1D3L

D1D2-ICAM-1 FULLY GLYCOSYLATED, VARIATION OF D1-D2 INTERDOMAIN ANGLE IN DIFFERENT CRYSTAL STRUCTURES.

1D3L の概要

• エントリーDOI: 10.2210/pdb1d3l/pdb
• 分子名称: PROTEIN (INTERCELLULAR ADHESION MOLECULE-1) (1 entity in total)
• 機能のキーワード: rhinovirus receptor, adhesion protein, glycoprotein, immunoglobulin fold, cell adhesion
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P05362
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20438.26

構造登録者

Bella, J.,Kolatkar, P.R.,Rossmann, M.G. (登録日: 1999-09-29, 公開日: 1999-12-01, 最終更新日: 2023-08-09)

主引用文献

Kolatkar, P.R.,Bella, J.,Olson, N.H.,Bator, C.M.,Baker, T.S.,Rossmann, M.G.
Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor.
EMBO J., 18:6249-6259, 1999

PubMed Abstract: Two human rhinovirus serotypes complexed with two- and five-domain soluble fragments of the cellular receptor, intercellular adhesion molecule-1, have been investigated by X-ray crystallographic analyses of the individual components and by cryo-electron microscopy of the complexes. The three-dimensional image reconstructions provide a molecular envelope within which the crystal structures of the viruses and the receptor fragments can be positioned with accuracy. The N-terminal domain of the receptor binds to the rhinovirus 'canyon' surrounding the icosahedral 5-fold axes. Fitting of molecular models into the image reconstruction density identified the residues on the virus that interact with those on the receptor surface, demonstrating complementarity of the electrostatic patterns for the tip of the N-terminal receptor domain and the floor of the canyon. The complexes seen in the image reconstructions probably represent the first stage of a multistep binding process. A mechanism is proposed for the subsequent viral uncoating process.

PubMed: 10562537
DOI: 10.1093/emboj/18.22.6249

実験手法

X-RAY DIFFRACTION (3.25 Å)