Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
3-DIMENSIONAL STRUCTURES OF THE FREE AND THE ANTIGEN-COMPLEXED FAB FROM MONOCLONAL ANTILYSOZYME ANTIBODY-D44.1
Autore:
BRADEN BC; SOUCHON H; EISELE JL; BENTLEY GA; BHAT TN; NAVAZA J; POLJAK RJ;
Indirizzi:
UNIV MARYLAND,MARYLAND BIOTECHNOL INST,CTR ADV RES BIOTECHNOL,9600 GUDELSKY DR ROCKVILLE MD 20850 UNIV MARYLAND,MARYLAND BIOTECHNOL INST,CTR ADV RES BIOTECHNOL ROCKVILLE MD 20850 INST PASTEUR F-75724 PARIS 15 FRANCE NCI,FCRFDC,CTR SUPERCOMP BIOMED,STRUCT BIOCHEM PROGRAM FREDERICK MD 21202
Titolo Testata:
Journal of Molecular Biology
fascicolo: 4, volume: 243, anno: 1994,
pagine: 767 - 781
SICI:
0022-2836(1994)243:4<767:3SOTFA>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNOGLOBULIN VARIABLE DOMAINS; X-RAY-DIFFRACTION; 3-DIMENSIONAL STRUCTURE; MACROMOLECULAR STRUCTURES; CRYSTAL-STRUCTURES; REFINEMENT; PROTEINS; CHAIN; CRYSTALLIZATION; NEURAMINIDASE;
Keywords:
MONOCLONAL ANTIBODY; 3-DIMENSIONAL STRUCTURE; ANTIGEN-ANTIBODY COMPLEX; CONFORMATIONAL CHANGE; X-RAY DIFFRACTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
55
Recensione:
Indirizzi per estratti:
Citazione:
B.C. Braden et al., "3-DIMENSIONAL STRUCTURES OF THE FREE AND THE ANTIGEN-COMPLEXED FAB FROM MONOCLONAL ANTILYSOZYME ANTIBODY-D44.1", Journal of Molecular Biology, 243(4), 1994, pp. 767-781

Abstract

The three-dimensional structures of the free and antigen-complexed Fabs from the mouse monoclonal anti-hen egg white lysozyme antibody D44.1 have been solved and refined by X-ray cr crystallographic techniques. The crystals of the free and lysozyme-bound Fabs were grown under identical conditions and their X-rag diffraction data were collected to 2.1 and 2.5 Angstrom, respectively. Two molecules of the Fab-lysozyme complex in the asymmetric unit of the crystals show nearly identical conformations and thus confirm the essential structural features of theantigen-antibody interface. Three buried water molecules enhance the surface complementarity at the interface and provide hydrogen bonds tostabilize the complex. Two hydrophobic buried holes are present at the interface which, although large enough to accommodate solvent molecules, are void. The combining site residues of the complexed FabD44.1 exhibit reduced temperature factors compared with those of the free Fab. Furthermore, small perturbations in atomic positions and rearrangements of side-chains at the combining site, and a relative rearrangementof the variable domains of the light (V-L) and the heavy (V-H) chains, detail a Fab accommodation of the bound lysozyme. The amino acid sequence of the V-H domain, as well as the epitope of lysozyme recognizedby D44.1 are very close to those previously reported for the monoclonal antibody HyHEL-5. A feature central to the FabD44.1 and FabHyHEL-5 complexes with lysozyme are three salt bridges between V-H glutamate residues 35 and 50 and lysozyme arginine residues 45 and 68. The presence of the three salt bridges in the D44.1-lysozyme inter face indicates that these bonds are not responsible for the 1000-fold increase in affinity for !yrsozyme that HyHEL-5 exhibits relative to D44.1.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 07:06:59