1RJC

Crystal structure of the camelid single domain antibody cAb-Lys2 in complex with hen egg white lysozyme

1RJC の概要

• エントリーDOI: 10.2210/pdb1rjc/pdb
• 関連するPDBエントリー: 1RI8
• 分子名称: camelid heavy chain antibody, Lysozyme C, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: beta sandwich, immunoglobulin fold, protein-protein hetero complex, alpha-beta orthogonal bundle, immune system-hydrolase complex, immune system/hydrolase
• 由来する生物種: Camelus dromedarius (Arabian camel); 詳細
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29420.52

構造登録者

De Genst, E.,Silence, K.,Ghahroudi, M.A.,Decanniere, K.,Loris, R.,Kinne, J.,Wyns, L.,Muyldermans, S. (登録日: 2003-11-19, 公開日: 2005-02-01, 最終更新日: 2024-11-20)

主引用文献

De Genst, E.,Silence, K.,Ghahroudi, M.A.,Decanniere, K.,Loris, R.,Kinne, J.,Wyns, L.,Muyldermans, S.
Strong in vivo maturation compensates for structurally restricted H3 loops in antibody repertoires.
J.Biol.Chem., 280:14114-14121, 2005

PubMed Abstract: A central paradigm in immunology states that successful generation of high affinity antibodies necessitates an immense primary repertoire of antigen-combining sites. Much of the diversity of this repertoire is provided by varying one antigen binding loop, created by inserting randomly a D (diversity) gene out of a small pool between the V and J genes. It is therefore assumed that any particular D-encoded region surrounded by different V and J regions adopts a different conformation. We have solved the structure of two lysozyme-specific variable domains of heavy-chain antibodies isolated from two strictly unrelated dromedaries. These antibodies recombined identical D gene sequences to different V and J precursors with significant variance in their V(D)J junctions. Despite these large differences, the D-encoded loop segments adopt remarkably identical architectures, thus directing the antibodies toward identical epitopes. Furthermore, a striking convergent maturation process occurred in the V region, adapting both binders for their sub-nanomolar affinity association with lysozyme. Hence, on a structural level, humoral immunity may rely more on well developed maturation and selection systems than on the acquisition of large primary repertoires.

PubMed: 15659390
DOI: 10.1074/jbc.M413011200

実験手法

X-RAY DIFFRACTION (1.4 Å)