NDLI: Engineering and characterization of a single chain surrogate light chain variable domain.

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Engineering and characterization of a single chain surrogate light chain variable domain.

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Engineering and characterization of a single chain surrogate light chain variable domain.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Bohm, Andrew Yüksel, Deniz Morstadt, Lucia Stollar, B. David Baleja, James D. Kumar, Krishna
Description	Country affiliation: United States Author Affiliation: Morstadt L ( Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.)
Abstract	The surrogate light chain (SLC) is a key regulator of B cell development in the bone marrow, resulting in mature B cells that produce antibodies that are capable of interacting with antigens. The SLC comprises two noncovalently interacting proteins: VpreB and 14.1. We engineered a construct to represent the complete immunoglobulin-like domain of the SLC variable domain in a single protein chain that could be bacterially expressed. In this construct, the incomplete immunoglobulin domain of VpreB (residues 1-102) was linked to the J-segment of 14.1 (residues 40-53), which provided one beta-strand to complete the V-like domain (VpreBJ). Because VpreBJ has the interface to VH chains, but lacks the unique region of 14.1, which is important for SLC signaling, we predict that a properly folded VpreBJ would have the potential to act as a dominant negative mutant of the surrogate light chain. X-ray crystallography of VpreBJ at 2.0 A resolution showed that the engineering was successful. With its two beta-pleated sheets, packed face-to-face, the single chain VpreBJ resembles a mature light chain immunoglobulin V-domain (VL). The surface that would normally interact with the VH chain interacts with a crystallographically related VpreBJ molecule. The presence of dimeric species in solution was verified by analytical ultracentrifugation. VpreBJ is easily overexpressed in bacteria, while retaining the native conformation of an immunoglobulin domain, and thus may serve as an important reagent for future studies in B-cell development.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1110/ps.073269808
Journal	Protein Science
Issue Number	3
Volume Number	17
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2008-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Immunoglobulin Light Chains, Surrogate Chemistry Immunoglobulin Variable Region Amino Acid Sequence Complementarity Determining Regions Crystallography, X-ray Dimerization Escherichia Coli Genetics Metabolism Models, Molecular Molecular Sequence Data Protein Engineering Protein Structure, Tertiary Sequence Alignment Research Support, N.i.h., Extramural Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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