2003
DOI: 10.1002/jmr.610
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Comparison of the three‐dimensional structures of a human Bence‐Jones dimer crystallized on Earth and aboard US Space Shuttle Mission STS‐95

Abstract: Crystals of a human (Sea) Bence-Jones dimer were produced in a capillary by vapor diffusion under microgravity conditions in the 9 day US Space Shuttle Mission STS-95. In comparison to ground-based experiments, nucleation was facile and spontaneous in space. Appearance of a very large (8 x 1.6 x 1.0 mm) crystal in a short time period is a strong endorsement for the use of microgravity to produce crystals sufficiently large for neutron diffraction studies. The Sea dimer crystallized in the orthorhombic space gr… Show more

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Cited by 12 publications
(10 citation statements)
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References 35 publications
(43 reference statements)
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“…In full-length LCs, V L s are connected to C L s through a joining (J) segment, which provides the domains with the flexibility to acquire conformations independent of each other. Such an architecture of the protein does not impose a particular orientation on V L s relative to connected C L s, as affirmed by the existence of several crystal structures (42,52,53). Therefore, a dimer of V L s maintains the ability to disassociate into amyloid-prone V L monomers, while still covalently attached to C L s. This flexibility explains why amyloid fibers of immunoglobulin can consist of fulllength LCs, just their V L s, or both.…”
Section: Discussionmentioning
confidence: 88%
“…In full-length LCs, V L s are connected to C L s through a joining (J) segment, which provides the domains with the flexibility to acquire conformations independent of each other. Such an architecture of the protein does not impose a particular orientation on V L s relative to connected C L s, as affirmed by the existence of several crystal structures (42,52,53). Therefore, a dimer of V L s maintains the ability to disassociate into amyloid-prone V L monomers, while still covalently attached to C L s. This flexibility explains why amyloid fibers of immunoglobulin can consist of fulllength LCs, just their V L s, or both.…”
Section: Discussionmentioning
confidence: 88%
“…The substitution was made in the program XTALVIEW [27], and 500 cycles of energy minimization were conducted using the program CNS [28]. Molecular models of the CamTran007 antibody F(ab) light and heavy chains were made using the highly homologous chains from 1LHZ (chain A) [29] and 1AD9 (chain B) [30], respectively. The intact F(ab) was created by superimposing the light and heavy chains onto the F(ab) peptide from 1FSK, and then performing energy minimization of all side chain atoms in CNS.…”
Section: Molecular Modelingmentioning
confidence: 99%
“…Among the latter were amino-acid residues A28 (Asp), A53 (Val), B53 (Val), A156 (Asp) and B214 (Thr). The first two residues belong to CDR loops 1 and 2 and were also found to be in disallowed regions in the other crystal forms, as well as in other -type light-chain dimers (Furey et al, 1983;Ely et al, 1989;Huang, Ainsworth, Stevens et al, 1996;Terzyan et al, 2003). Torsional strain is possibly the cause of these frequent outliers, since they are involved in tight -type (CDR-1) and -type (CDR-2) turns.…”
Section: P4 3 2 1 2 Crystal Formmentioning
confidence: 92%
“…This angle may vary even among members of a single BJ population. A number of BJ protein structures have been determined using X-ray crystallography, each unique in sequence, antigen specificity, domain dispositions and other detailed features (Epp et al, 1975;Furey et al, 1983;Ely et al, 1989;Huang et al, 1994;Huang, Ainsworth, Solomon et al, 1996;Huang, Ainsworth, Stevens et al, 1996;Roussel et al, 1999;Terzyan et al, 2003).…”
Section: Introductionmentioning
confidence: 99%