Crystal structure of a human single domain antibody dimer formed through V H-V H non-covalent interactions

Toya Nath Baral, Shi Yu Chao, Shenghua Li, Jamshid Tanha, Mehdi Arbabi-Ghahroudi, Jianbing Zhang, Shuying Wang

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


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.

Original languageEnglish
Article numbere30149
JournalPloS one
Issue number1
Publication statusPublished - 2012 Jan 12

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

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