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Titolo:
Recognition of the nonpolar base 4-methylindole in DNA by the DNA repair adenine glycosylase MutY
Autore:
Chepanoske, CL; Langelier, CR; Chmiel, NH; David, SS;
Indirizzi:
Univ Utah, Dept Chem, Salt Lake City, UT 84112 USA Univ Utah Salt Lake City UT USA 84112 Chem, Salt Lake City, UT 84112 USA
Titolo Testata:
ORGANIC LETTERS
fascicolo: 9, volume: 2, anno: 2000,
pagine: 1341 - 1344
SICI:
1523-7060(20000504)2:9<1341:ROTNB4>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI MUTY; C-TERMINAL DOMAIN; EXCISION-REPAIR; SUBSTRATE-ANALOGS; STRUCTURAL BASIS; HYDROGEN-BONDS; ENZYME; SPECIFICITY; MISPAIRS; PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: David, SS Univ Utah, Dept Chem, 315 South 1400 East, Salt Lake City, UT 84112 USA Univ Utah 315 South 1400 East Salt Lake City UT USA 84112 12 USA
Citazione:
C.L. Chepanoske et al., "Recognition of the nonpolar base 4-methylindole in DNA by the DNA repair adenine glycosylase MutY", ORG LETT, 2(9), 2000, pp. 1341-1344

Abstract

The DNA repair adenine glycosylase MutY efficiently recognizes 7-deaza-2'-deoxyadenosine (Z) and its nonpolar isostere 4-methylindole beta-deoxynucleoside (M) opposite 7,8-dihydro-8-oxo-2'-deoxyguanosine (OG) and G in DNA. Both wild-type and truncated MutY exhibit a 10- to 20-fold higher affinity for a duplex containing OG:M than OG:Z, More efficient recognition of M overZ by MutY may be to due the lack of hydrogen bonding with the OG that facilitates nucleotide flipping during the substrate recognition process.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 06:27:59