Characterization and preliminary crystallographic data on the VL-related fragment of the human kI Bence Jones protein Wat |
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Authors: | F J Stevens F A Westholm N Panagiotopoulos M Schiffer R A Popp A Solomon |
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Affiliation: | Division of Biological and Medical Research Argonne National Laboratory Argonne, IL, 60439, U.S.A.;Biology Division Oak Ridge National Laboratory Oak Ridge, TN, 37830, U.S.A.;Departments of Medical Biology and Medicine College of Medicine and Memorial Research Center University of Tennessee Center for the Health Sciences Knoxville, TN, 37920, U.S.A. |
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Abstract: | A “naturally occurring” human κI VL dimer, designated Wat, has been isolated and crystallized. Protein Wat consists of two non-covalently bound monomers, each having a molecular weight of ~ 11,500. The monomer subunit is composed of an entire variable region light chain (VL) domain closely homologous to that of the κI Bence Jones protein Roy (Hilschmann &; Craig, 1965) as evidenced from amino acid composition, tryptic peptide map, and sequence analysis. Immunochemical studies substantiated that protein Wat is of the κ chain subgroup κI and lacks the isotypic and allotypic antigenic determinants associated with the κ constant region light chain domain. Two types of crystals of VL dimer Wat were obtained from ammonium sulfate or polyethylene glycol solutions. The type I crystals have unit cell dimensions of , and the space group is hexagonal P62 or P64. The asymmetric unit consists of one VL dimer; the fractional volume of unit cell occupied by solvent is 0.51. The unit cell dimensions of the type II crystals are ; the space group is hexagonal P6122 or P6522. Three variable domains constitute the asymmetric unit of the type II crystals; the fractional value of the solvent (0.52) is compatible with the value obtained for the type I crystals. |
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Keywords: | Protein Bhe was classified serologically as having a V region sequence characteristic of Al light chains based on immunochemical analyses of material furnished by Dr B. C. Wang. |
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