1SL6

Crystal Structure of a fragment of DC-SIGNR (containg the carbohydrate recognition domain and two repeats of the neck) complexed with Lewis-x.

1SL6 の概要

• エントリーDOI: 10.2210/pdb1sl6/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900120
• 分子名称: C-type lectin DC-SIGNR, alpha-L-fucopyranose-(1-3)-[beta-D-galactopyranose-(1-4)]2-acetamido-2-deoxy-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: dc-signr, c-type lectin, sugar binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 132565.85

構造登録者

Guo, Y.,Feinberg, H.,Conroy, E.,Mitchell, D.A.,Alvarez, R.,Blixt, O.,Taylor, M.E.,Weis, W.I.,Drickamer, K. (登録日: 2004-03-05, 公開日: 2004-06-15, 最終更新日: 2024-10-30)

主引用文献

Guo, Y.,Feinberg, H.,Conroy, E.,Mitchell, D.A.,Alvarez, R.,Blixt, O.,Taylor, M.E.,Weis, W.I.,Drickamer, K.
Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR
Nat.Struct.Mol.Biol., 11:591-598, 2004

PubMed Abstract: Both the dendritic cell receptor DC-SIGN and the closely related endothelial cell receptor DC-SIGNR bind human immunodeficiency virus and enhance infection. However, biochemical and structural comparison of these receptors now reveals that they have very different physiological functions. By screening an extensive glycan array, we demonstrated that DC-SIGN and DC-SIGNR have distinct ligand-binding properties. Our structural and mutagenesis data explain how both receptors bind high-mannose oligosaccharides on enveloped viruses and why only DC-SIGN binds blood group antigens, including those present on microorganisms. DC-SIGN mediates endocytosis, trafficking as a recycling receptor and releasing ligand at endosomal pH, whereas DC-SIGNR does not release ligand at low pH or mediate endocytosis. Thus, whereas DC-SIGN has dual ligand-binding properties and functions both in adhesion and in endocytosis of pathogens, DC-SIGNR binds a restricted set of ligands and has only the properties of an adhesion receptor.

PubMed: 15195147
DOI: 10.1038/nsmb784

実験手法

X-RAY DIFFRACTION (2.25 Å)