Symmetry, stability, and dynamics of multidomain and multicomponent protein systems

被引：85

作者：

Blundell, TL

Srinivasan, N

机构：

[1] Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, Tennis Court Road

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1996年 / 93卷 / 25期

基金：

英国惠康基金;

关键词：

D O I：

10.1073/pnas.93.25.14243

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：

Symmetry is commonly observed in many biological systems. Here we discuss representative examples of the role of symmetry in structural molecular biology. Point group symmetries are observed in many protein oligomers whose three-dimensional atomic structures have been elucidated by x-ray crystallography. Approximate symmetry also occurs in multidomain proteins. Symmetry often confers stability on the molecular system and results in economical usage of basic components to build the macromolecular structure. Symmetry is also associated with cooperativity. Mild perturbation from perfect symmetry mag be essential in some systems for dynamic functions.

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页码：14243 / 14248

页数：6

相关论文

共 69 条

[1]

[Anonymous], 1952, GROWTH FORM

[2] THE STRUCTURE OF TRP RNA-BINDING ATTENUATION PROTEIN [J].

ANTSON, AA ;

OTRIDGE, J ;

BRZOZOWSKI, AM ;

DODSON, EJ ;

DODSON, GG ;

WILSON, KS ;

SMITH, TM ;

YANG, M ;

KURECKI, T ;

GOLLNICK, P .

NATURE, 1995, 374 (6524) :693-700

[3] Circular assemblies [J].

Antson, AA ;

Dodson, EJ ;

Dodson, GG .

CURRENT OPINION IN STRUCTURAL BIOLOGY, 1996, 6 (02) :142-150

[4] THE STRUCTURE OF 2ZN PIG INSULIN CRYSTALS AT 1.5-A RESOLUTION [J].

BAKER, EN ;

BLUNDELL, TL ;

CUTFIELD, JF ;

CUTFIELD, SM ;

DODSON, EJ ;

DODSON, GG ;

HODGKIN, DMC ;

HUBBARD, RE ;

ISAACS, NW ;

REYNOLDS, CD ;

SAKABE, K ;

SAKABE, N ;

VIJAYAN, NM .

PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES, 1988, 319 (1195) :369-&

[5] Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex [J].

Banerjee, R ;

Das, K ;

Ravishankar, R ;

Suguna, K ;

Surolia, A ;

Vijayan, M .

JOURNAL OF MOLECULAR BIOLOGY, 1996, 259 (02) :281-296

[6] STRUCTURE OF CHICKEN MUSCLE TRIOSE PHOSPHATE ISOMERASE DETERMINED CRYSTALLOGRAPHICALLY AT 2.5A RESOLUTION USING AMINO-ACID SEQUENCE DATA [J].

BANNER, DW ;

BLOOMER, AC ;

PETSKO, GA ;

PHILLIPS, DC ;

POGSON, CI ;

WILSON, IA ;

CORRAN, PH ;

FURTH, AJ ;

MILMAN, JD ;

OFFORD, RE ;

PRIDDLE, JD ;

WALEY, SG .

NATURE, 1975, 255 (5510) :609-614

[7] X-RAY-ANALYSIS OF BETA-B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS [J].

BAX, B ;

LAPATTO, R ;

NALINI, V ;

DRIESSEN, H ;

LINDLEY, PF ;

MAHADEVAN, D ;

BLUNDELL, TL ;

SLINGSBY, C .

NATURE, 1990, 347 (6295) :776-780

[8] PROTEIN DISK OF TOBACCO MOSAIC-VIRUS AT 2.8-A RESOLUTION SHOWING INTERACTIONS WITHIN AND BETWEEN SUBUNITS [J].

BLOOMER, AC ;

CHAMPNESS, JN ;

BRICOGNE, G ;

STADEN, R ;

KLUG, A .

NATURE, 1978, 276 (5686) :362-368

[9] THE MOLECULAR-STRUCTURE AND STABILITY OF THE EYE LENS - X-RAY-ANALYSIS OF GAMMA-CRYSTALLIN-II [J].

BLUNDELL, T ;

LINDLEY, P ;

MILLER, L ;

MOSS, D ;

SLINGSBY, C ;

TICKLE, I ;

TURNELL, B ;

WISTOW, G .

NATURE, 1981, 289 (5800) :771-777

[10]

Blundell T, 1972, ADV PROTEIN CHEM, V1972, P279, DOI 10.1016/S0065-3233(08)60143-6

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