1MAM

CRYSTAL STRUCTURE TO 2.45 A RESOLUTION OF A MONOCLONAL FAB SPECIFIC FOR THE BRUCELLA A CELL WALL POLYSACCHARIDE ANTIGEN

1MAM の概要

• エントリーDOI: 10.2210/pdb1mam/pdb
• 分子名称: IGG2B-KAPPA YST9.1 FAB (LIGHT CHAIN), IGG2B-KAPPA YST9.1 FAB (HEAVY CHAIN) (2 entities in total)
• 機能のキーワード: immunoglobulin
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Isoform 1: Cell membrane; Single-pass membrane protein (Potential). Isoform 2: Secreted: P01867
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46929.01

構造登録者

Rose, D.R. (登録日: 1992-01-14, 公開日: 1993-10-31, 最終更新日: 2024-10-23)

主引用文献

Rose, D.R.,Przybylska, M.,To, R.J.,Kayden, C.S.,Oomen, R.P.,Vorberg, E.,Young, N.M.,Bundle, D.R.
Crystal structure to 2.45 A resolution of a monoclonal Fab specific for the Brucella A cell wall polysaccharide antigen.
Protein Sci., 2:1106-1113, 1993

PubMed Abstract: The atomic structure of an antibody antigen-binding fragment (Fab) at 2.45 A resolution shows that polysaccharide antigen conformation and Fab structure dictated by combinatorial diversity and domain association are responsible for the fine specificity of the Brucella-specific antibody, YsT9.1. It discriminates the Brucella abortus A antigen from the nearly identical Brucella melitensis M antigen by forming a groove-type binding site, lined with tyrosine residues, that accommodates the rodlike A antigen but excludes the kinked structure of the M antigen, as envisioned by a model of the antigen built into the combining site. The variable-heavy (VH) and variable-light (VL) domains are derived from genes closely related to two used in previously solved structures, M603 and R19.9, respectively. These genes combine in YsT9.1 to form an antibody of totally different specificity. Comparison of this X-ray structure with a previously built model of the YsT9.1 combining site based on these homologies highlights the importance of VL:VH association as a determinant of specificity and suggests that small changes at the VL:VH interface, unanticipated in modeling, may cause significant modulation of binding-site properties.

PubMed: 8358294

実験手法

X-RAY DIFFRACTION (2.45 Å)