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Titolo:
A role of the third complementarity-determining region in the affinity maturation of an antibody
Autore:
Furukawa, K; Shirai, H; Azuma, T; Nakamura, H;
Indirizzi:
Sci Univ Tokyo, Res Inst Biol Sci, Chiba 2780022, Japan Sci Univ Tokyo Chiba Japan 2780022 s Inst Biol Sci, Chiba 2780022, Japan Tokyo Med & Dent Univ, Med Res Inst, Bunkyo Ku, Tokyo 1138510, Japan TokyoMed & Dent Univ Tokyo Japan 1138510 unkyo Ku, Tokyo 1138510, Japan Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England Univ Cambridge Cambridge England CB2 1GA hem, Cambridge CB2 1GA, England Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan Osaka Univ Suita Osaka Japan 5650871 rot Res, Suita, Osaka 5650871, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 29, volume: 276, anno: 2001,
pagine: 27622 - 27628
SICI:
0021-9258(20010720)276:29<27622:AROTTC>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
SOMATIC HYPERMUTATION; JUNCTIONAL DIVERSITY; GERMINAL-CENTERS; N-REGIONS; B-CELLS; IMMUNOGLOBULIN; GENERATION; RESPONSES; MUTATION; PROGRAM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Furukawa, K Sci Univ Tokyo, Res Inst Biol Sci, 2669 Yamazaki, Chiba 2780022, Japan Sci Univ Tokyo 2669 Yamazaki Chiba Japan 2780022 80022, Japan
Citazione:
K. Furukawa et al., "A role of the third complementarity-determining region in the affinity maturation of an antibody", J BIOL CHEM, 276(29), 2001, pp. 27622-27628

Abstract

We recently found that there are two distinct antibody maturation pathwaysfor the immune response of C57BL/6 mice to (4-hydroxy-3-nitrophenyl) acetyl and that a junctional amino acid introduced at a point far in advance of somatic hypermutation determined which pathway of affinity maturation was used. We describe here the structural basis for this aspect of maturation using recently developed H3 rules, which allow for reliable identification ofthe conformation of the third complementarity-determining region of the heavy chain (CDR-H3) from the primary amino acid sequences only. By the application of these rules, the anti-(4-hydroxy-3-nitrophenyl) acetyl antibodiesexamined here were classified into two major groups on the basis of their CDR-H3 structure, and these groups were found to be consistent with the maturation pathways. In addition, circular dichroism measurements revealed that the versatile nature-of the antigen binding of the antibodies was significantly influenced by the pathway employed. We postulated in this study thatflexibility in the CDR-H3 structure in the antigen-combining site could facilitate efficient antibody maturation supported by a plurality of possibleantigen binding modes.

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Documento generato il 20/01/21 alle ore 02:51:39