3QYC

Structure of a dimeric anti-HER2 single domain antibody

3QYC の概要

• エントリーDOI: 10.2210/pdb3qyc/pdb
• 分子名称: VH domain of IgG molecule (2 entities in total)
• 機能のキーワード: immunoglobulin v domain fold, antibody, immune system
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31480.83

構造登録者

Baral, T.N.,Chao, S.,Li, S.,Tanha, J.,Arbabai, M.,Wang, S.,Zhang, J. (登録日: 2011-03-03, 公開日: 2012-02-08, 最終更新日: 2024-11-20)

主引用文献

Baral, T.N.,Chao, S.Y.,Li, S.,Tanha, J.,Arbabi-Ghahroudi, M.,Zhang, J.,Wang, S.
Crystal Structure of a Human Single Domain Antibody Dimer Formed through V(H)-V(H) Non-Covalent Interactions.
Plos One, 7:e30149-e30149, 2012

PubMed Abstract: Single-domain antibodies (sdAbs) derived from human V(H) are considered to be less soluble and prone to aggregate which makes it difficult to determine the crystal structures. In this study, we isolated and characterized two anti-human epidermal growth factor receptor-2 (HER2) sdAbs, Gr3 and Gr6, from a synthetic human V(H) phage display library. Size exclusion chromatography and surface plasmon resonance analyses demonstrated that Gr3 is a monomer, but that Gr6 is a strict dimer. To understand this different molecular behavior, we solved the crystal structure of Gr6 to 1.6 Å resolution. The crystal structure revealed that the homodimer assembly of Gr6 closely mimics the V(H)-V(L) heterodimer of immunoglobulin variable domains and the dimerization interface is dominated by hydrophobic interactions.

PubMed: 22253912
DOI: 10.1371/journal.pone.0030149

実験手法

X-RAY DIFFRACTION (1.6 Å)