¹⁵N, ¹³C and ¹H resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody.
Heavy chain antibodies differ in structure to conventional antibodies lacking both the light chain and the first heavy chain constant domain (CH1). Characteristics of the antigen-binding variable heavy domain of the heavy chain antibody (VHH) including the smaller size, high solubility and stability make them an attractive alternative to more traditional antibody fragments for detailed NMR-based structural analysis. Here we report essentially complete backbone and side chain (15)N, (13)C and (1)H assignments for a free VHH. Analysis of the backbone chemical shift data obtained indicates that the VHH is comprised predominantly of β-sheets corresponding to nearly 60% of the protein backbone.
Department of Biochemistry, Henry Wellcome Building, University of Leicester, Lancaster Road, Leicester, LE1 9HN, UK, cep23@le.ac.uk.
Christine E
CE
Prosser
Lorna C
LC
Waters
Frederick W
FW
Muskett
Vaclav
V
Veverka
Philip W
PW
Addis
Laura M
LM
Griffin
Terry S
TS
Baker
Alastair D G
AD
Lawson
Ulrich
U
Wernery
Jorg
J
Kinne
Alistair J
AJ
Henry
Richard J
RJ
Taylor
Mark D
MD
Carr
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000737:chemistry*; D002162:Camelus; D002247:Carbon Isotopes; D006859:Hydrogen; D007143:Immunoglobulin Heavy Chains / Q000737:chemistry*; D007135:Immunoglobulin Variable Region / Q000737:chemistry*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D000906:Antibodies; D002247:Carbon Isotopes; D007143:Immunoglobulin Heavy Chains; D007135:Immunoglobulin Variable Region; D009587:Nitrogen Isotopes; D006859:Hydrogen