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Titolo:
Binding of synthetic peptides by a human monoclonal IgM with an unusual combining site structure
Autore:
Edmundson, AB; Tribbick, G; Plompen, S; Geysen, HM; Yuriev, E; Ramsland, PA;
Indirizzi:
Oklahoma Med Res Fdn, Crystallog Program, Oklahoma City, OK 73104 USA Oklahoma Med Res Fdn Oklahoma City OK USA 73104 lahoma City, OK 73104 USA Chiron Mimotopes Pty Ltd, Clayton, Vic, Australia Chiron Mimotopes Pty Ltd Clayton Vic Australia , Clayton, Vic, Australia Glaxo Wellcome Inc, Res Triangle Pk, NC 27709 USA Glaxo Wellcome Inc Res Triangle Pk NC USA 27709 Triangle Pk, NC 27709 USA
Titolo Testata:
JOURNAL OF MOLECULAR RECOGNITION
fascicolo: 4, volume: 14, anno: 2001,
pagine: 229 - 238
SICI:
0952-3499(200107/08)14:4<229:BOSPBA>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
B-CELL REPERTOIRE; ANTIGENIC DETERMINANTS; NATURAL AUTOANTIBODIES; CONTINUOUS EPITOPES; AMINO-ACID; MOUSE IGG; ANTIBODIES; PROTEIN; IMMUNOGLOBULIN; PREDICTION;
Keywords:
antibodies; combinatorial chemistry; IgM; synthetic peptides; antibody-peptide recognition;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Edmundson, AB Oklahoma Med Res Fdn, Crystallog Program, 825 NE 13th St, Oklahoma City, OK 73104 USA Oklahoma Med Res Fdn 825 NE 13th St Oklahoma CityOK USA 73104
Citazione:
A.B. Edmundson et al., "Binding of synthetic peptides by a human monoclonal IgM with an unusual combining site structure", J MOL RECOG, 14(4), 2001, pp. 229-238

Abstract

Using X-ray crystallography, a human monoclonal IgM cryoglobulin (Mez) wasfound to have an unusual combining site topography. Analysis of the unliganded Fv at 2.6 Angstrom resolution revealed that the HCDR3 had partitioned the active site into two compartments [Ramsland PA et al 2000. Mol Immunol.37: 295-310]. The two cavities had dimensions and chemical properties thatwere compatible with the binding of peptides. In this study, libraries of peptides were prepared using solid-phase synthesis. Binding of the intact Mez IgM to these peptides was tested by enzyme-linked immunoassays. Screening of 400 dipeptides revealed that binding was markedly skewed toward amino acids with aromatic side-chains (Phe and Trp), especially when located in the second position. Preferential recognition of aromatic side-chains by MezIgM was confirmed with larger peptides of three to five residues, but C-terminal positioning was not favored in these peptides. Mez IgM also showed binding propensities for acidic residues (Asp and Glu) as well as several other sidechains with different chemical properties, including His, Pro, Asn and Gln. Mez IgM recognized sets of overlapping octapeptides representing the sequences of the constant domains of human IgG1 heavy chains. These peptides represented similar stretches of polypeptide on the three-dimensional structures of all three constant domains (CHI, CH2 and CH3). Thus, Mez IgM may recognize structurally homologous regions of immunoglobulin domains, which were conserved during the evolution of the immune system. Copyright, (C) 2001 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 09:48:40