2HRL

Siglec-7 in complex with GT1b

2HRL の概要

• エントリーDOI: 10.2210/pdb2hrl/pdb
• 関連するPDBエントリー: 1O7S 1O7V 2DF3 2G5R
• 分子名称: Sialic acid-binding Ig-like lectin 7, N-acetyl-alpha-neuraminic acid-(2-8)-N-acetyl-alpha-neuraminic acid-(2-3)-[2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: ig-like domain, siglec, ganglioside, siglec-7, 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: Q9Y286
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16106.75

構造登録者

Attrill, H.,Imamura, A.,Sharma, R.S.,Kiso, M.,Crocker, P.R.,van Aalten, D.M.F. (登録日: 2006-07-20, 公開日: 2006-08-15, 最終更新日: 2024-10-30)

主引用文献

Attrill, H.,Imamura, A.,Sharma, R.S.,Kiso, M.,Crocker, P.R.,van Aalten, D.M.F.
Siglec-7 Undergoes a Major Conformational Change When Complexed with the {alpha}(2,8)-Disialylganglioside GT1b
J.Biol.Chem., 281:32774-32783, 2006

PubMed Abstract: The siglecs are a group of mammalian sialic acid binding receptors expressed predominantly in the immune system. The CD33-related siglecs show complex recognition patterns for sialylated glycans. Siglec-7 shows a preference for alpha(2,8)-disialylated ligands and provides a structural template for studying the key interactions that drive this selectivity. We have co-crystallized Siglec-7 with a synthetic oligosaccharide corresponding to the alpha(2,8)-disialylated ganglioside GT1b. The crystal structure of the complex offers a first glimpse into how this important family of lectins binds the structurally diverse gangliosides. The structure reveals that the C-C' loop, a region implicated in previous studies as driving siglec specificity, undergoes a dramatic conformational shift, allowing it to interact with the underlying neutral glycan core of the ganglioside. The structural data in combination with mutagenesis studies show that binding of the ganglioside is driven by extensive hydrophobic contacts together with key polar interactions and that the binding site structure is complementary to preferred solution conformations of GT1b.

PubMed: 16895906
DOI: 10.1074/jbc.M601714200

実験手法

X-RAY DIFFRACTION (1.85 Å)