3QYC

Structure of a dimeric anti-HER2 single domain antibody

Summary for 3QYC

• Entry DOI: 10.2210/pdb3qyc/pdb
• Descriptor: VH domain of IgG molecule (2 entities in total)
• Functional Keywords: immunoglobulin v domain fold, antibody, immune system
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 31480.83

Authors

Baral, T.N.,Chao, S.,Li, S.,Tanha, J.,Arbabai, M.,Wang, S.,Zhang, J. (deposition date: 2011-03-03, release date: 2012-02-08, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)