1CLZ

IGG FAB (IGG3, KAPPA) FRAGMENT (MBR96) COMPLEXED WITH LEWIS Y NONOATE METHYL ESTER

1CLZ の概要

• エントリーDOI: 10.2210/pdb1clz/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900054
• 分子名称: IGG FAB (IGG3, KAPPA), alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, METHYL NONANOATE (ESTER), ... (4 entities in total)
• 機能のキーワード: immunoglobulin c region, glycoprotein, transmembrane, immunoglobulin
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48854.56

構造登録者

Sheriff, S.,Bajorath, J. (登録日: 1995-03-15, 公開日: 1996-08-01, 最終更新日: 2024-10-30)

主引用文献

Jeffrey, P.D.,Bajorath, J.,Chang, C.Y.,Yelton, D.,Hellstrom, I.,Hellstrom, K.E.,Sheriff, S.
The x-ray structure of an anti-tumour antibody in complex with antigen.
Nat.Struct.Biol., 2:466-471, 1995

PubMed Abstract: The crystal structures of the murine BR96 Fab and its human chimera have been determined in complex with the nonoate methyl ester derivative of Lewis Y (nLey) at 2.8 A and 2.5 A resolution, respectively. BR96 binds the carbohydrate in a large pocket which is formed by residues of all CDR loops except L2. The binding of the carbohydrate is mediated predominantly by aromatic residues in BR96. Analysis of the structure suggests that BR96 is capable of recognizing a structure larger than the Le(y) tetrasaccharide, providing a possible explanation for its high tumour selectivity. The structure provides a rationale for mutagenesis experiments that have resulted in BR96 CDR loop mutants with increased affinity for nLey and/or tumour cells.

PubMed: 7664109
DOI: 10.1038/nsb0695-466

実験手法

X-RAY DIFFRACTION (2.8 Å)