Match!

Preliminary crystallographic data on the human λIII Bence Jones protein dimer Cle

Published on Mar 1, 1981in Journal of Molecular Biology5.067
· DOI :10.1016/0022-2836(81)90085-1
Fred J. Stevens31
Estimated H-index: 31
(Argonne National Laboratory),
Florence A. Westholm7
Estimated H-index: 7
(Argonne National Laboratory)
+ 2 AuthorsMarianne Schiffer40
Estimated H-index: 40
(Argonne National Laboratory)
Abstract
A complete human λ Bence Jones protein dimer (Cle) has been isolated and crystallized. Protein Cle was characterized immunochemically and chemically as having a variable region amino acid sequence associated with light chains of the λ chain subgroup, λIII, and a constant region sequence characteristic of “non-Mcg” type λ chains. Bence Jones protein Cle contains two covalently bound intact monomers, each having a molecular weight of ~23,000. Crystals of Bence Jones protein Cle, obtained from ammonium sulfate solutions, diffract to 2.6 A resolution and have the orthorhombic space group P212121 with cell dimensions a = 113.0 A, b = 72.3 A, and c = 48.9 A. The asymmetric unit consists of a dimer with a molecular weight of ~ 46,000.
  • References (12)
  • Citations (3)
📖 Papers frequently viewed together
3 Citations
1995
2 Authors (M. Schiffer, D.B. Huang)
21 Citations
78% of Scinapse members use related papers. After signing in, all features are FREE.
References12
Newest
#1Bi-Cheng Wang (University of Pittsburgh)H-Index: 48
#2C. S. Yoo (University of Pittsburgh)H-Index: 8
Last. Martin Sax (University of Pittsburgh)H-Index: 21
view all 3 authors...
Abstract The crystal structure of protein Rhe, a lambda type V L dimer, has been determined at a resolution of 3 A by the method of multiple isomorphous replacement supplemented with anomalous scattering data. A crystallographic sequence was assigned from an interpretation of the electron density map in an optical comparator and is compared with a chemically determined partial amino acid sequence. The monomeric unit of Rhe, as determined crystallographically, contains 113 amino acids, 110 belong...
24 CitationsSource
#1Marianne Schiffer (Argonne National Laboratory)H-Index: 40
#2Florence A. Westholm (Argonne National Laboratory)H-Index: 7
Last. Alan Solomon (UT: University of Tennessee)H-Index: 30
view all 4 authors...
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 ...
3 CitationsSource
#1Michael Laughrea (Yale University)H-Index: 6
#2Peter B. Moore (Yale University)H-Index: 40
Abstract 30 S ribosomal subunits in many preparations have two binding sites for S1 (Laughrea & Moore, 1977). These two binding sites can be readily distinguished on the basis of their affinity for S1. Reactivation procedures (Zamir et al. , 1971) selectively modify the interaction of the 30 S subunit with S1: the weaker binding site disappears but the affinity of the stronger stays unchanged. Experiments performed to identify molecular components of S1's binding site(s) on the 30 S subunit have...
36 CitationsSource
#1Masaaki Matsushima (MPG: Max Planck Society)H-Index: 20
#2Markus Marquart (MPG: Max Planck Society)H-Index: 5
Last. Walter Palm (University of Graz)H-Index: 9
view all 7 authors...
The crystal structure of the Fab‡ fragment of the IgG protein Kol was analysed and an electron density map calculated at 3 A resolution based on phases obtained from multiple isomorphous replacement. An atomic model was constructed but the lack of amino acid sequence data causes some uncertainty, in particular concerning the amino acid side-chains. Several cycles of constrained crystallographic refinement (Deisenhofer & Steigemann, 1975) produced an R value of 0.36. The resulting model was compa...
51 CitationsSource
#1Alan Solomon (UT: University of Tennessee)H-Index: 30
The availability of antisera with specificity forλ light chains which have the Mcg- or the non-Mcg-associated amino acid C-region sequence alternations has made possible our immunochemical differentiation of humanλ chains as Mcg+ or Mcg−. One antiserum, prepared against an Mcg+ λ chain having the Mcg-associated C-region amino acid residues (asparaginyl, threonyl, and lysyl at positions 116, 118, and 167, respectively), had specificity forλ chains with this C-region sequence. A second antiserum, ...
8 CitationsSource
#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
view all 6 authors...
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
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
#1O. EppH-Index: 22
#2Eaton E. LattmanH-Index: 33
Last. Walter PalmH-Index: 9
view all 5 authors...
: 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...
218 CitationsSource
#1Allen B. EdmundsonH-Index: 35
#2Kathryn R. ElyH-Index: 19
Last. N. PanagiotopoulosH-Index: 3
view all 5 authors...
208 CitationsSource
#1Marianne SchifferH-Index: 40
#2Rowland L. GirlingH-Index: 3
Last. Allen B. EdmundsonH-Index: 35
view all 4 authors...
289 CitationsSource
Cited By3
Newest
#1G. Boulot (Pasteur Institute)H-Index: 14
#2V. Guillon (Pasteur Institute)H-Index: 2
Last. Diana Tello (Pasteur Institute)H-Index: 14
view all 8 authors...
Abstract Immunoglobulins, myeloma light chains and their fragments, and Fab fragments from monoclonal antibodies of predefined specificity have been crystallized as single components or complexed with their specific antigens. The intersegmental flexibility of antibody molecules has imposed the strategy of attempting to crystallize their Fab and Fc fragments separately. Intrasegmental mobility in Fabs has not been an obstacle to their crystallization, although this has been a low frequency event,...
6 CitationsSource
#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
view all 3 authors...
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...
17 CitationsSource
#1Chong Hwan ChangH-Index: 3
#2Michael T. ShortH-Index: 2
Last. Marianne SchifferH-Index: 40
view all 8 authors...
: 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...
50 CitationsSource