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1ieh

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{{STRUCTURE_1ieh| PDB=1ieh | SCENE= }}
{{STRUCTURE_1ieh| PDB=1ieh | SCENE= }}
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'''SOLUTION STRUCTURE OF A SOLUBLE SINGLE-DOMAIN ANTIBODY WITH HYDROPHOBIC RESIDUES TYPICAL OF A VL/VH INTERFACE'''
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===SOLUTION STRUCTURE OF A SOLUBLE SINGLE-DOMAIN ANTIBODY WITH HYDROPHOBIC RESIDUES TYPICAL OF A VL/VH INTERFACE===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 12093273 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12093273}}
==About this Structure==
==About this Structure==
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEH OCA].
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Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEH OCA].
==Reference==
==Reference==
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[[Category: Immunoglobulin beta-barrel]]
[[Category: Immunoglobulin beta-barrel]]
[[Category: Two pleated beta-sheet]]
[[Category: Two pleated beta-sheet]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:50:47 2008''

Revision as of 07:50, 1 July 2008

Image:1ieh.png

Template:STRUCTURE 1ieh

SOLUTION STRUCTURE OF A SOLUBLE SINGLE-DOMAIN ANTIBODY WITH HYDROPHOBIC RESIDUES TYPICAL OF A VL/VH INTERFACE

Template:ABSTRACT PUBMED 12093273

About this Structure

Full experimental 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

Page seeded by OCA on Tue Jul 1 10:50:47 2008

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