Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions

被引:836
作者
Tompa, Peter [1 ]
Fuxreiter, Monika [1 ]
机构
[1] Hungarian Acad Sci, Biol Res Ctr, Inst Enzymol, Budapest, Hungary
基金
英国惠康基金; 匈牙利科学研究基金会;
关键词
D O I
10.1016/j.tibs.2007.10.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The notion that all protein functions are determined through macromolecular interactions is the driving force behind current efforts that aim to solve the structures of all cellular complexes. Recent findings, however, demonstrate a significant amount of structural disorder or polymorphism in protein complexes, a phenomenon that has been largely overlooked thus far. It is our view that such disorder can be classified into four mechanistic categories, covering a continuous spectrum of structural states from static to dynamic disorder and from segmental to full disorder. To emphasize its generality and importance, we suggest a generic term, 'fuzziness', for this phenomenon. Given the crucial role of protein disorder in protein-protein interactions and in regulatory processes, we envision that fuzziness will become integral to understanding the interactome.
引用
收藏
页码:2 / 8
页数:7
相关论文
共 58 条
[1]   Structural systems biology: modelling protein interactions [J].
Aloy, P ;
Russell, RB .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2006, 7 (03) :188-197
[2]   Ten thousand interactions for the molecular biologist [J].
Aloy, P ;
Russell, RB .
NATURE BIOTECHNOLOGY, 2004, 22 (10) :1317-1321
[3]   CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices [J].
Baker, Jennifer M. R. ;
Hudson, Rhea P. ;
Kanelis, Voula ;
Choy, Wing-Yiu ;
Thibodeau, Patrick H. ;
Thomas, Philip J. ;
Forman-Kay, Julie D. .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2007, 14 (08) :738-745
[4]   The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway [J].
Bhattacharyya, RP ;
Reményi, A ;
Good, MC ;
Bashor, CJ ;
Falick, AM ;
Lim, WA .
SCIENCE, 2006, 311 (5762) :822-826
[5]   Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity [J].
Borg, Mikael ;
Mittag, Tanja ;
Pawson, Tony ;
Tyers, Mike ;
Forman-Kay, Julie D. ;
Chan, Hue Sun .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (23) :9650-9655
[6]   The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded [J].
Bourhis, JM ;
Receveur-Bréchot, V ;
Oglesbee, M ;
Zhang, XS ;
Buccellato, M ;
Darbon, H ;
Canard, B ;
Finet, S ;
Longhi, S .
PROTEIN SCIENCE, 2005, 14 (08) :1975-1992
[7]   Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90 [J].
Cliff, MJ ;
Harris, R ;
Barford, D ;
Ladbury, JE ;
Williams, MA .
STRUCTURE, 2006, 14 (03) :415-426
[8]  
Dunker A K, 2000, Genome Inform Ser Workshop Genome Inform, V11, P161
[9]   Intrinsically unstructured proteins and their functions [J].
Dyson, HJ ;
Wright, PE .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2005, 6 (03) :197-208
[10]   Coupling of folding and binding for unstructured proteins [J].
Dyson, HJ ;
Wright, PE .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2002, 12 (01) :54-60