3HNS

CS-35 Fab Complex with Oligoarabinofuranosyl Hexasaccharide

3HNS の概要

• エントリーDOI: 10.2210/pdb3hns/pdb
• 関連するPDBエントリー: 3HNT 3HNV
• 分子名称: CS-35 Fab Heavy Chain, CS-35 Fab Light Chain, beta-D-arabinofuranose-(1-2)-alpha-D-arabinofuranose-(1-3)-[beta-D-arabinofuranose-(1-2)-alpha-D-arabinofuranose-(1-5)]alpha-D-arabinofuranose-(1-5)-methyl alpha-D-arabinofuranoside, ... (4 entities in total)
• 機能のキーワード: antibody-carbohydrate complex, oligofuranoside, tuberculosis, immune system
• 由来する生物種: Mus musculus (mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48346.72

構造登録者

Murase, T.,Zheng, R.B.,Joe, M.,Bai, Y.,Marcus, S.L.,Lowary, T.L.,Ng, K.K.S. (登録日: 2009-06-01, 公開日: 2009-07-21, 最終更新日: 2024-11-27)

主引用文献

Murase, T.,Zheng, R.B.,Joe, M.,Bai, Y.,Marcus, S.L.,Lowary, T.L.,Ng, K.K.
Structural insights into antibody recognition of mycobacterial polysaccharides.
J.Mol.Biol., 392:381-392, 2009

PubMed Abstract: Mycobacteria are major human pathogens responsible for such serious and widespread diseases as tuberculosis and leprosy. Among the evolutionary adaptations essential for pathogenicity in mycobacteria is a complex carbohydrate-rich cell-wall structure that contains as a major immunomodulatory molecule the polysaccharide lipoarabinomannan (LAM). We report here crystal structures of three fragments from the non-reducing termini of LAM in complex with a murine antibody Fab fragment (CS-35Fab). These structures reveal for the first time the three-dimensional structures of key components of LAM and the molecular basis of LAM recognition at between 1.8- and 2.0-A resolution. The antigen-binding site of CS-35Fab forms three binding pockets that show a high degree of complementarity to the reducing end, the branch point and one of the non-reducing ends of the Y-shaped hexasaccharide moiety found at most of the non-reducing termini of LAM. Structures of CS-35Fab bound to two additional tetrasaccharides confirm the general mode of binding seen in the hexasaccharide and indicate how different parts of LAM are recognized. Altogether, these structures provide a rational basis for understanding the overall architecture of LAM and identify the key elements of an epitope that may be exploited for the development of novel and more effective anti-mycobacterial vaccines. Moreover, this study represents the first high-resolution X-ray crystallographic investigation of oligofuranoside-protein recognition.

PubMed: 19577573
DOI: 10.1016/j.jmb.2009.06.074

実験手法

X-RAY DIFFRACTION (2 Å)