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Volumn 273, Issue 5281, 1996, Pages 1539-1541

A protein phosphorylation switch at the conserved allosteric site in GP

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE 6 PHOSPHATE; GLYCOGEN PHOSPHORYLASE;

EID: 0029783651     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.273.5281.1539     Document Type: Article
Times cited : (80)

References (30)
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    • P. D. Boyer and E. G. Krebs, Eds. Academic Press, New York
    • E. G. Krebs, in The Enzymes, P. D. Boyer and E. G. Krebs, Eds. (Academic Press, New York, 1986), vol. 17, pp. 3-20.
    • (1986) The Enzymes , vol.17 , pp. 3-20
    • Krebs, E.G.1
  • 6
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    • S. R. Sprang et al., Nature 336, 215 (1988).
    • (1988) Nature , vol.336 , pp. 215
    • Sprang, S.R.1
  • 14
    • 9544249431 scopus 로고    scopus 로고
    • note
    • The procedures for the purification and phosphorylation of yeast GP were as previously described (13). The details of crystallization and structure determination will be presented elsewhere (16).
  • 15
    • 9544222663 scopus 로고    scopus 로고
    • note
    • 2-termini bind, and the catalytic face, on the opposite side, where the substrates enter.
  • 17
    • 0021009969 scopus 로고
    • -10-Gly-Phe-Leu, respectively, where the residues undergoing reversible phosphorylation are numbered. The yeast GP is efficiently phosphorylated by a cyclic adenosine 3′,5′-monophosphate-dependent protein kinase, whereas the mammalian GP is recognized by a highly specific GP kinase [D. J. Graves, Methods Enzymol. 99, 268 (1983)].
    • (1983) Methods Enzymol. , vol.99 , pp. 268
    • Graves, D.J.1
  • 23
    • 9544228368 scopus 로고    scopus 로고
    • in preparation
    • 2-terminus becomes disordered in that structure (K. Lin et al., in preparation).
    • Lin, K.1
  • 25
    • 0029029617 scopus 로고
    • P. D. Jeffrey et al., Nature 376, 313 (1995).
    • (1995) Nature , vol.376 , pp. 313
    • Jeffrey, P.D.1
  • 27
  • 29
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    • Supplementary information is available at the authors' Web site: http://util.ucsf.edu/flett/lin/science. html.
  • 30
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    • note
    • We thank I. Herskowitz, A. Weiss, M. M. Crerar, and S. L. Slatin for critical reading and discussion of the manuscript, and D. Singler for the art work. Supported by NIH grant DK32822 to R.J.F. K.L. is a Burroughs Wellcome Fund Fellow of the Life Sciences Research Foundation.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.