1MEL

CRYSTAL STRUCTURE OF A CAMEL SINGLE-DOMAIN VH ANTIBODY FRAGMENT IN COMPLEX WITH LYSOZYME

1MEL の概要

• エントリーDOI: 10.2210/pdb1mel/pdb
• 分子名称: VH SINGLE-DOMAIN ANTIBODY, LYSOZYME (3 entities in total)
• 機能のキーワード: camel single-domain anti-lysozyme, complex (antibody-antigen), complex (antibody-antigen) complex, complex (antibody/antigen)
• 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: 4
• 化学式量合計: 59976.50

構造登録者

Desmyter, A.,Transue, T.R.,Arbabi Gharoudi, M.,Dao Thi, M.,Poortmans, F.,Hamers, R.,Muyldermans, S.,Wyns, L. (登録日: 1996-06-06, 公開日: 1997-06-16, 最終更新日: 2024-10-30)

主引用文献

Desmyter, A.,Transue, T.R.,Ghahroudi, M.A.,Thi, M.H.,Poortmans, F.,Hamers, R.,Muyldermans, S.,Wyns, L.
Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme.
Nat.Struct.Biol., 3:803-811, 1996

PubMed Abstract: The Camelidae is the only taxonomic family known to possess functional heavy-chain antibodies, lacking light chains. We report here the 2.5 A resolution crystal structure of a camel VH in complex with its antigen, lysozyme. Compared to human and mouse VH domains, there are no major backbone rearrangements in the VH framework. However, the architecture of the region of VH that interacts with a VL in a conventional FV is different from any previously seen. Moreover, the CDR1 region, although in sequence homologous to human CDR1, deviates fundamentally from the canonical structure. Additionally, one half of the CDR3 contacts the VH region which in conventional immunoglobulins interacts with a VL whereas the other half protrudes from the antigen binding site and penetrates deeply into the active site of lysozyme.

PubMed: 8784355
DOI: 10.1038/nsb0996-803

実験手法

X-RAY DIFFRACTION (2.5 Å)