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Immunoglobulin variable domains

Stevens PW, Raffen R, Hanson DK, Deng YL, Berrios Hammond M, Westholm FA, Murphy C, Eulitz M, Wetzel R, Solomon A, et al. Recombinant immunoglobulin variable domains generated from synthetic genes provide a system for in vitro characterization of light-chain amyloid proteins. Protein Sci 1995 4 421-432. [Pg.276]

Orlandi, R., Gussow, D.H., Jones, P.T., and Winteg G. (1989) Cloning immunoglobulin variable domains for expression by the polymerase chain reaction. Proc. Natl. Acad. Sci. USA 86, 3833-3837. [Pg.1100]

Figure 31-5 The extensive conserved hydrogen-bonding pattern in an immunoglobulin variable domain provided by polar residues buried inside the VL and VH domains. (A) To facilitate orientation, prominent side chains are displayed here and identified by names and numbers in the same orientation as in (B). (B) Polypeptide chain backbones of both domains are denoted by heavy lines and hydrogen bonds by light lines. In addition to the regular interbackbone hydrogen-bonding network characteristic of antiparallel (3-sheets, there are hydrogen bonds provided by side-chain atoms. Note the two hydrogen bonds of Gln-38 (VL) and Gin-39 (VH) that span the domain—domain interface. From Novotny and Haber.75... Figure 31-5 The extensive conserved hydrogen-bonding pattern in an immunoglobulin variable domain provided by polar residues buried inside the VL and VH domains. (A) To facilitate orientation, prominent side chains are displayed here and identified by names and numbers in the same orientation as in (B). (B) Polypeptide chain backbones of both domains are denoted by heavy lines and hydrogen bonds by light lines. In addition to the regular interbackbone hydrogen-bonding network characteristic of antiparallel (3-sheets, there are hydrogen bonds provided by side-chain atoms. Note the two hydrogen bonds of Gln-38 (VL) and Gin-39 (VH) that span the domain—domain interface. From Novotny and Haber.75...
Ward, E S., Gussow, D., Griffiths, A. D., Jones, P T, and Winter, G. (1989) Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature 341, 544—546... [Pg.424]

The TCR is a member of the immunoglobulin superfamily and is composed of an N-terminal immunoglobulin variable domain, an immunoglobulin constant... [Pg.21]

Immunoglobulin variable domain Tolerates loss of structural disulfide bridge Error-prone PCR... [Pg.151]

Idiotype. Unique, genetically controlled determinants present on immunoglobulin variable domains and that determine the... [Pg.239]

Figure 4. "Richardson diagrams" [29] of five proteins illustrating four classes of tertiary-fold motifs typically found in globular proteins, (a) AU-a hemoglobin, P subunit, (b) AU- Immunoglobulin variable domain, (c) o/p tnose phosphate isomerase. (d) ot/p alcohol dehydrogenase, domain 2. (e) a+ Stai ylococcal nuclease. Figure 4. "Richardson diagrams" [29] of five proteins illustrating four classes of tertiary-fold motifs typically found in globular proteins, (a) AU-a hemoglobin, P subunit, (b) AU- Immunoglobulin variable domain, (c) o/p tnose phosphate isomerase. (d) ot/p alcohol dehydrogenase, domain 2. (e) a+ Stai ylococcal nuclease.
Fig. 2.50. Comparison of step-by-step build-up of backbone configurations for superoxide dismutase (down the left side) and an immunoglobulin variable domain (down the right side). New backbone added at each step is shown by heavy arrows (from Richardson et al., 1976). Fig. 2.50. Comparison of step-by-step build-up of backbone configurations for superoxide dismutase (down the left side) and an immunoglobulin variable domain (down the right side). New backbone added at each step is shown by heavy arrows (from Richardson et al., 1976).

See other pages where Immunoglobulin variable domains is mentioned: [Pg.622]    [Pg.112]    [Pg.1021]    [Pg.1373]    [Pg.224]    [Pg.964]    [Pg.558]    [Pg.583]    [Pg.1020]    [Pg.627]    [Pg.144]    [Pg.148]    [Pg.151]    [Pg.2177]    [Pg.2181]   
See also in sourсe #XX -- [ Pg.3 , Pg.2181 ]




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Variable domains

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