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Crystallographic data on a complete κ-type human Bence-Jones protein☆

Published on Sep 1, 1978in Journal of Molecular Biology5.067
· DOI :10.1016/0022-2836(78)90161-4
Marianne Schiffer40
Estimated H-index: 40
(Argonne National Laboratory),
Florence A. Westholm7
Estimated H-index: 7
(Argonne National Laboratory)
+ 1 AuthorsAlan Solomon30
Estimated H-index: 30
(UT: University of Tennessee)
Abstract
Abstract A complete human κ-type Bence—Jones protein (Fin) has been isolated and crystallized. Immunochemical and physicochemical characterization of protein Fin indicates that it is of the κ-chain subgroup, κII, and that it consists of two non-covalently bound intact monomers having a molecular weight of ~23,000 Crystals of Bence—Jones protein Fin obtained from ammonium sulfate solutions have the orthorhombic space group P2 1 2 1 2 1 with cell dimensions a = 132.0 A , b = 93.3 A , and c = 42.3 A . The asymmetric unit consists of a dimer of molecular weight ~46,000.
  • References (16)
  • Citations (3)
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References16
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#1Bi-Cheng Wang (University of Pittsburgh)H-Index: 48
#2C. S. Yoo (University of Pittsburgh)H-Index: 8
Last. M. Michaels (Allegheny General Hospital)H-Index: 1
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A Bence-Jones protein, Pav, was isolated from the urine of a myeloma patient. Crystals were grown by five different methods yielding different morphologies with slightly changed cell parameters, but the space group was the same (P212121) in every case and X-ray patterns appeared to be identical. The cell parameters are: a = 93.6 (4) to 95.1(4) A, b = 92.7(3) A and c = 72.8(2) A. The crystal density and solvent content are approximately 1.128 g/cm3 and 0.64, respectively. Chemical evidence sugges...
5 CitationsSource
#1Peter M. Colman (USYD: University of Sydney)H-Index: 64
#2H.J. Schramm (MPG: Max Planck Society)H-Index: 3
Last. J.M. Guss (USYD: University of Sydney)H-Index: 15
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Abstract The crystal and molecular structure of the dimer of variable domains of the Bence-Jones protein ROY has been determined by Patterson function search procedures, using the known structure of the protein REI. The structure has been partially refined at 3.0 A resolution to a crystallographic R -factor value of 0.33. One of the 18 residues differentiating ROY from REI is the substitution of Tyr96 for Leu96, a substitution which makes the combining site of the ROY dimer larger. Substantial m...
32 CitationsSource
Various exemplary embodiments, devices, systems, and methods for sensing moisture are disclosed, including at least one moisture sensor that comprises an optical fiber, a long period grating formed in at least a portion of the optical fiber, and a layer of PEI bonded to the long period grating. One exemplary embodiment comprises a system for measuring humidity, the system comprising an optical fiber moisture sensor having a mono-layer of PEI covalently-bonded to an outer surface of said optical ...
148 CitationsSource
#1Fumio KishidaH-Index: 2
#2Takachika AzumaH-Index: 22
Last. Kozo HamaguchiH-Index: 28
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: The formation of the interchain disulfide bonds in partially reduced Bence Jones proteins and immunoglobulins was studied in the presence of glutathione. It was found that only oxidized glutathione (GSSG) was effective for the formation of the interchain disulfide bonds in type gamma Bence Jones proteins and IgG. In type kappa Bence Jones proteins, on the other hand, no formation of the inter L-L disulfide bond was observed in the presence of GSSG at above pH 6. The kinetic pattern of disulfid...
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#1O. EppH-Index: 22
#2Eaton E. LattmanH-Index: 33
Last. Walter PalmH-Index: 9
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: The structure of the variable portions of a K-type Bence-Jones protein REI forming a dimer has been determined by X-ray diffraction to a resolution of 2.0 A. The structure has been refined using a constrained crystallographic refinement procedure. The final R value is 0.24 for 15000 significantly measured reflections; the estimated standard deviation of atomic positions is 0.09 A. A more objective assessment of the error in the atomic positions is possible by comparing the two independently re...
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#1Allen B. EdmundsonH-Index: 35
#2Kathryn R. ElyH-Index: 19
Last. N. PanagiotopoulosH-Index: 3
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#1Heinz FehlhammerH-Index: 8
#2Marianne SchifferH-Index: 40
Last. H.J. Schramm (MPG: Max Planck Society)H-Index: 3
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The structure of a χ-type Bence-Jones protein variable fragment Au has been determined by molecular replacement methods using the known structure of an other Bence-Jones variable fragment Rei (Epp et al., Eur. J. Biochem. 45, 513 (1974)). The crystallographic R factor is 0.31 for about 4000 significantly measured reflections between 6.8 to 2.5 a. The Au protein forms a dimer across a crystallographic two fold axis. The spatial relationship of the two monomers, the conformation of the backbones a...
48 CitationsSource
#1O. Epp (MPG: Max Planck Society)H-Index: 22
#2Peter M. Colman (MPG: Max Planck Society)H-Index: 64
Last. Walter Palm (MPG: Max Planck Society)H-Index: 9
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The structure of the variable part of a χ-type Bence-Jones protein RE1 has been determined at a resolution of 0.28 nm. It forms a dimer in the crystal related by a local diad, held together by hydrogen bonding interactions of residues Tyr-36, Gln-38, Ala-43, Pro-44, Tyr-87, Gln-89 and Phe-98, which are largely conserved in light chains. The structure consists of two hydrogen-bonded sheets covering a hydrophobic interior made up of mostly conserved amino-acid side chains. Approximately 50% of the...
194 CitationsSource
#1Carla L. McLaughlin (UT: University of Tennessee)H-Index: 12
#2Alan Solomon (UT: University of Tennessee)H-Index: 30
An antigenic site, which was not immunochemically demonstrable in the intact κ light polypeptide chain, was exposed by enzymatic cleavage of the κ chain into its variant half and constant half. This antigenic site located in the constant region the κ chain was detected immunochemically by several antiserums that had specificity for this site. Treatment of an intact κ chain with a dissociating agent resulted in the exposure of the hidden antigenic site, which was as readily detected in the unfold...
11 CitationsSource
Abstract The evaluation of numerous anti-κ chain antisera through immunochemical studies of κ light chains for which complete or partial sequence data were available has resulted in the localization of three distinct regions in the variant half of the light chain which are associated with specific antigenic sites. The residue at position 9 appears to be associated with an antigenic site which, in general, may be termed a group-related antigenic site. The residues at positions 45 and 94 through 9...
30 Citations
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#1Marianne Schiffer (Argonne National Laboratory)H-Index: 40
#2C.-H. Chang (Argonne National Laboratory)H-Index: 12
Last. Fred J. Stevens (Argonne National Laboratory)H-Index: 31
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Abstract The packing interactions in crystals of human λ-type antibody light chain dimers have been reviewed. These homologous proteins are composed of individually specific variable domains, but all have very similar constant domain sequences. The proteins do not emulate each other in their overall crystallization behavior: each attains an individually characteristic space group or unit cell dimensions. However, each of these protein crystals has one unit cell dimension in common, 72.4(± 0.2) A...
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#1Chong Hwan ChangH-Index: 3
#2Michael T. ShortH-Index: 2
Last. Marianne SchifferH-Index: 40
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: We have characterized and crystallized a human lambda I light-chain dimer, Bence-Jones protein Loc, which has variable (V) region antigenic determinants characteristic for the lambda I subgroup and constant (C) region determinants of the C lambda I gene Mcg. The crystal structure was determined to 3-A resolution; the R factor is 0.27. The angle formed by the twofold axes of the V and C domains, the "elbow bend", is 97 degrees, the smallest found so far for an antibody fragment. The antigen-bin...
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#1Fred J. Stevens (Argonne National Laboratory)H-Index: 31
#2Florence A. Westholm (Argonne National Laboratory)H-Index: 7
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