5ILT

Crystal structure of bovine Fab A01

5ILT の概要

• エントリーDOI: 10.2210/pdb5ilt/pdb
• 関連するPDBエントリー: 5E99 5IHU 5IJV
• 分子名称: bovine Fab A01 light chain, bovine Fab A01 heavy chain (3 entities in total)
• 機能のキーワード: antibody fab ultralong cdr h3, immune system
• 由来する生物種: Bos taurus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51410.68

構造登録者

Stanfield, R.L.,Wilson, I.A. (登録日: 2016-03-04, 公開日: 2016-08-24, 最終更新日: 2024-11-20)

主引用文献

Stanfield, R.L.,Wilson, I.A.,Smider, V.V.
Conservation and diversity in the ultralong third heavy-chain complementarity-determining region of bovine antibodies.
Sci Immunol, 1:-, 2016

PubMed Abstract: A subset of bovine antibodies have an exceptionally long third heavy-chain complementarity determining region (CDR H3) that is highly variable in sequence and includes multiple cysteines. These long CDR H3s (up to 69 residues) fold into a long stalk atop which sits a knob domain that is located far from the antibody surface. Three new bovine Fab crystal structures have been determined to decipher the conserved and variable features of ultralong CDR H3s that lead to diversity in antigen recognition. Despite high sequence variability, the stalks adopt a conserved β-ribbon structure, while the knob regions share a conserved β-sheet that serves as a scaffold for two connecting loops of variable length and conformation, as well as one conserved disulfide. Variation in patterns and connectivity of the remaining disulfides contribute to the knob structural diversity. The unusual architecture of these ultralong bovine CDR H3s for generating diversity is unique in adaptive immune systems.

PubMed: 27574710
DOI: 10.1126/sciimmunol.aaf7962

実験手法

X-RAY DIFFRACTION (2 Å)