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PDBsum entry 1ieh
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Immune system
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PDB id
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1ieh
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Solution structure of a llama single-Domain antibody with hydrophobic residues typical of the vh/vl interface.
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Authors
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W.Vranken,
D.Tolkatchev,
P.Xu,
J.Tanha,
Z.Chen,
S.Narang,
F.Ni.
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Ref.
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Biochemistry, 2002,
41,
8570-8579.
[DOI no: ]
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PubMed id
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Abstract
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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.
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