Literature DB >> 1695509

Antigen-antibody interactions: an NMR approach.

P E Wright1, H J Dyson, R A Lerner, L Riechmann, P Tsang.   

Abstract

With recent advances in methodology, it now appears that NMR can be used at an unprecedented level of sophistication to obtain new insights into the solution structure and dynamics of the antibody combining site, both free and in its complex with antigen. Most promising in this regard is the Fv fragment (molecular weight approximately 25 kD) which can be produced by genetic engineering in a form suitable for NMR studies. Isotopic labeling is required to make specific resonance assignments. NMR can also provide information on the conformational preferences of immunogenic peptides and can be used to probe the conformation and dynamics of peptides (appropriately labeled with 13C or 15N) bound to the Fab fragment (molecular weight approximately 50 kD) of antipeptide antibodies.

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Year:  1990        PMID: 1695509     DOI: 10.1016/0006-2952(90)90182-k

Source DB:  PubMed          Journal:  Biochem Pharmacol        ISSN: 0006-2952            Impact factor:   5.858


  5 in total

1.  Production and characterization of 22 monoclonal antibodies directed against S 20499, a new potent 5-HT1A chiral agonist: influence of the hapten structure on specificity and stereorecognition.

Authors:  P Got; E Raimbaud; C Bussey; G Caron; P A Carrupt; B Walther; A Bensussan; J M Scherrmann
Journal:  Pharm Res       Date:  1999-05       Impact factor: 4.200

2.  Identification of the epitopes of calcitonin gene-related peptide (CGRP) for two anti-CGRP monoclonal antibodies by 2D NMR.

Authors:  J A Hubbard; D P Raleigh; J R Bonnerjea; C M Dobson
Journal:  Protein Sci       Date:  1997-09       Impact factor: 6.725

3.  Specific fluorine labeling of the HyHEL10 antibody affects antigen binding and dynamics.

Authors:  Mauro Acchione; Yi-Chien Lee; Morgan E DeSantis; Claudia A Lipschultz; Alexander Wlodawer; Mi Li; Aranganathan Shanmuganathan; Richard L Walter; Sandra Smith-Gill; Joseph J Barchi
Journal:  Biochemistry       Date:  2012-07-16       Impact factor: 3.162

4.  Backbone assignment, secondary structure and protein A binding of an isolated, human antibody VH domain.

Authors:  L Riechmann; J Davies
Journal:  J Biomol NMR       Date:  1995-09       Impact factor: 2.835

5.  Aliphatic 1H and 13C resonance assignments for the 26-10 antibody VL domain derived from heteronuclear multidimensional NMR spectroscopy.

Authors:  K L Constantine; V Goldfarb; M Wittekind; M S Friedrichs; J Anthony; S C Ng; L Mueller
Journal:  J Biomol NMR       Date:  1993-01       Impact factor: 2.835

  5 in total

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