1QFO

N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE) IN COMPLEX WITH 3'SIALYLLACTOSE

1QFO の概要

• エントリーDOI: 10.2210/pdb1qfo/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900025
• 分子名称: PROTEIN (SIALOADHESIN), N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose, N-acetyl-alpha-neuraminic acid, ... (4 entities in total)
• 機能のキーワード: immunoglobulin superfamily, carbohydrate binding, immune system
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 41533.69

構造登録者

May, A.P.,Robinson, R.C.,Vinson, M.,Crocker, P.R.,Jones, E.Y. (登録日: 1999-04-12, 公開日: 1999-04-16, 最終更新日: 2024-10-30)

主引用文献

May, A.P.,Robinson, R.C.,Vinson, M.,Crocker, P.R.,Jones, E.Y.
Crystal structure of the N-terminal domain of sialoadhesin in complex with 3' sialyllactose at 1.85 A resolution.
Mol.Cell, 1:719-728, 1998

PubMed Abstract: The structure of the functional N-terminal domain from the extracellular region of the cell surface receptor sialoadhesin has been determined in complex with the oligosaccharide 3' sialyllactose. This provides structural information for the siglec family of proteins. The structure conforms to the V-set immunoglobulin-like fold but contains several distinctive features, including an intra-beta sheet disulphide and a splitting of the standard beta strand G into two shorter strands. These novel features appear important in adapting the V-set fold for sialic acid-mediated recognition. Analysis of the complex with 3'sialyllactose highlights three residues, conserved throughout the siglec family, as key features of the sialic acid-binding template. The complex is representative of the functional recognition interaction with carbohydrate and as such provides detailed information for a heterotypic cell adhesion interaction.

PubMed: 9660955
DOI: 10.1016/S1097-2765(00)80071-4

実験手法

X-RAY DIFFRACTION (1.85 Å)