1ieh
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(New page: 200px<br /> <applet load="1ieh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ieh" /> '''SOLUTION STRUCTURE OF A SOLUBLE SINGLE-DOMA...)
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Revision as of 07:25, 18 November 2007
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SOLUTION STRUCTURE OF A SOLUBLE SINGLE-DOMAIN ANTIBODY WITH HYDROPHOBIC RESIDUES TYPICAL OF A VL/VH INTERFACE
Overview
The three-dimensional structure of a llama single-domain antibody BrucD4-4, was established by use of solution NMR spectroscopy. BrucD4-4 has Val, Gly, Leu, and Trp residues at positions 37, 44, 45, and 47, which are, considered to be a hallmark to distinguish llama VH from V(H)H fragments, at the germline level. In contrast to the murine and human VHs, BrucD4-4, has sufficient solubility, is monomeric in solution, and displays, high-quality NMR spectra characteristic of well-structured proteins. Amide, proton/deuterium exchange and the (15)N relaxation data showed that, BrucD4-4 has a classic protein structure with a well-packed core and, comparatively mobile surface loops. The three-dimensional architecture of, BrucD4-4 is analogous to that of VHs from murine and human F(v)s and, camelid V(H)Hs with two pleated beta-sheets formed by four and five, beta-strands. A canonical and undistorted beta-barrel exposes a number of, hydrophobic residues into the solvent on the surface of the, three-dimensional structure. The eight-residue H3 loop folds over the side, chain of Val37 similarly to that in llama V(H)Hs; however, this, interaction may be transient due to the H3 conformational flexibility., Overall, the surface characteristics of BrucD4-4 with respect to, hydrophobicity appear to lie between the human VH domain from Fv Pot and, the llama V(H)H fragment HC-V, which may explain its enhanced solubility, allowing NMR structural analysis.
About this Structure
1IEH is a Protein complex structure of sequences from Lama glama. Full crystallographic information is available from OCA.
Reference
Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface., Vranken W, Tolkatchev D, Xu P, Tanha J, Chen Z, Narang S, Ni F, Biochemistry. 2002 Jul 9;41(27):8570-9. PMID:12093273
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