1MEL

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

Summary for 1MEL

• Entry DOI: 10.2210/pdb1mel/pdb
• Descriptor: VH SINGLE-DOMAIN ANTIBODY, LYSOZYME (3 entities in total)
• Functional Keywords: camel single-domain anti-lysozyme, complex (antibody-antigen), complex (antibody-antigen) complex, complex (antibody/antigen)
• Biological source: Camelus dromedarius (Arabian camel); More
• Cellular location: Secreted: P00698
• Total number of polymer chains: 4
• Total formula weight: 59976.50

Authors

Desmyter, A.,Transue, T.R.,Arbabi Gharoudi, M.,Dao Thi, M.,Poortmans, F.,Hamers, R.,Muyldermans, S.,Wyns, L. (deposition date: 1996-06-06, release date: 1997-06-16, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)