Active site-directed protein regulation

被引：166
作者：
Kobe, B [1 ]
Kemp, BE [1 ]
机构：
[1] St Vincents Inst Med Res, Fitzroy, Vic 3065, Australia
来源：
NATURE | 1999年 / 402卷 / 6760期
关键词：
D O I：
10.1038/46478
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Regulation of protein function is vital for the control of cellular processes. Proteins are often regulated by allosteric mechanisms, in which effecters bind to regulatory sites distinct from the active sites and alter protein function. Intrasteric regulation, directed at the active site and thus the counterpart of allosteric control, is now emerging as an important regulatory mechanism.
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页码：373 / 376
页数：4
相关论文
共 46 条
[1]   The structure and mechanism of protein phosphatases: Insights into catalysis and regulation [J].
Barford, D ;
Das, AK ;
Egloff, MP .
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE, 1998, 27 :133-164
[2]   Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization [J].
Bilwes, AM ;
denHertog, J ;
Hunter, T ;
Noel, JP .
NATURE, 1996, 382 (6591) :555-559
[3]   NATURAL PROTEIN PROTEINASE-INHIBITORS AND THEIR INTERACTION WITH PROTEINASES [J].
BODE, W ;
HUBER, R .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1992, 204 (02) :433-451
[4]   Activation mechanism of the MAP kinase ERK2 by dual phosphorylation [J].
Canagarajah, BJ ;
Khokhlatchev, A ;
Cobb, MH ;
Goldsmith, EJ .
CELL, 1997, 90 (05) :859-869
[5]   Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction [J].
Carr, PD ;
Verger, D ;
Ashton, AR ;
Ollis, DL .
STRUCTURE, 1999, 7 (04) :461-475
[6]   THE PROTEIN-KINASE DOMAIN OF THE ANP RECEPTOR IS REQUIRED FOR SIGNALING [J].
CHINKERS, M ;
GARBERS, DL .
SCIENCE, 1989, 245 (4924) :1392-1394
[7]  
CIGNOLANI G, 1999, NATURE, V399, P221
[8]   Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin α [J].
Conti, E ;
Uy, M ;
Leighton, L ;
Blobel, G ;
Kuriyan, J .
CELL, 1998, 94 (02) :193-204
[9]   CRYSTAL-STRUCTURE OF BOVINE TRYPSINOGEN AT 1.8 A RESOLUTION .2. CRYSTALLOGRAPHIC REFINEMENT, REFINED CRYSTAL-STRUCTURE AND COMPARISON WITH BOVINE TRYPSIN [J].
FEHLHAMMER, H ;
BODE, W ;
HUBER, R .
JOURNAL OF MOLECULAR BIOLOGY, 1977, 111 (04) :415-438
[10]   CHYMOTRYPSINOGEN - 2.5-A CRYSTAL STRUCTURE, COMPARISON WITH ALPHA-CHYMOTRYPSIN, AND IMPLICATIONS FOR ZYMOGEN ACTIVATION [J].
FREER, ST ;
KRAUT, J ;
ROBERTUS, JD ;
WRIGHT, HT ;
XUONG, NH .
BIOCHEMISTRY, 1970, 9 (09) :1997-&
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