Disordered Proteinaceous Machines

被引:95
作者
Fuxreiter, Monika [1 ]
Toth-Petroczy, Agnes [2 ]
Kraut, Daniel A. [3 ]
Matouschek, Andreas T. [4 ]
Lim, Roderick Y. H. [5 ]
Xue, Bin [6 ,8 ]
Kurgan, Lukasz [9 ]
Uversky, Vladimir N. [7 ,10 ]
机构
[1] Univ Debrecen, Dept Biochem & Mol Biol, MTA DE Momentum Lab Prot Dynam, H-4032 Debrecen, Hungary
[2] Weizmann Inst Sci, Dept Biol Chem, IL-7610001 Rehovot, Israel
[3] Villanova Univ, Dept Chem, Villanova, PA 19085 USA
[4] Univ Texas Austin, Inst Cellular & Mol Biol, Sect Mol Genet & Microbiol, Austin, TX 78712 USA
[5] Univ Basel, Biozentrum & Swiss Nanosci Inst, CH-4056 Basel, Switzerland
[6] Univ S Florida, Coll Fine Arts & Sci, Dept Cell Biol Microbiol & Mol Biol, Tampa, FL 33612 USA
[7] Univ S Florida, Dept Mol Med, Tampa, FL 33612 USA
[8] Univ S Florida, Morsani Coll Med, USF Hlth Byrd Alzheimers Res Inst, Tampa, FL 33612 USA
[9] Univ Alberta, Dept Elect & Comp Engn, Edmonton, AB T6G 2R3, Canada
[10] Russian Acad Sci, Inst Biol Instrumentat, Pushchino 119991, Moscow Region, Russia
关键词
NUCLEAR-PORE COMPLEX; RNA-POLYMERASE-II; GENE-SPECIFIC TRANSCRIPTION; MEDIATOR HEAD MODULE; INTRINSICALLY UNSTRUCTURED PROTEINS; UBIQUITIN-PROTEASOME SYSTEM; NATIVELY UNFOLDED PROTEINS; LARGE RIBOSOMAL-SUBUNIT; CELL-CYCLE PROGRESSION; AMINO-ACID-COMPOSITION;
D O I
10.1021/cr4007329
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Functions of IDPs/IDPRs may arise from a specific disordered form, from interconversion between disordered forms, and from transitions between disordered and ordered states. The choice between these states is determined by the specific protein environment. Many IDPs possess an exceptional ability to fold in a template-dependent manner, where a single IDPR can bind to multiple partners gaining very different structures in the bound state. Composition-based classification takes into account a simple fact that the polypeptide chains involved in the complex formation can be identical or nonidentical, thereby giving raise to homo- and hetero-oligomers. Geometrically, units of the homo-oligomers can be organized isologously or heterologously, where isologous association involves the same surface on both monomers of the homo-oligomer, and an heterologous association relies on different interfaces.
引用
收藏
页码:6806 / 6843
页数:38
相关论文
共 511 条
[91]   Signal transduction via unstructured protein conduits [J].
Dunker, A. Keith ;
Uversky, Vladimir N. .
NATURE CHEMICAL BIOLOGY, 2008, 4 (04) :229-230
[92]   The unfoldomics decade: an update on intrinsically disordered proteins [J].
Dunker, A. Keith ;
Oldfield, Christopher J. ;
Meng, Jingwei ;
Romero, Pedro ;
Yang, Jack Y. ;
Chen, Jessica Walton ;
Vacic, Vladimir ;
Obradovic, Zoran ;
Uversky, Vladimir N. .
BMC GENOMICS, 2008, 9 (Suppl 2)
[93]   Function and structure of inherently disordered proteins [J].
Dunker, A. Keith ;
Silman, Israel ;
Uversky, Vladimir N. ;
Sussman, Joel L. .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2008, 18 (06) :756-764
[94]   Flexible nets - The roles of intrinsic disorder in protein interaction networks [J].
Dunker, AK ;
Cortese, MS ;
Romero, P ;
Iakoucheva, LM ;
Uversky, VN .
FEBS JOURNAL, 2005, 272 (20) :5129-5148
[95]   The protein trinity - linking function and disorder [J].
Dunker, AK ;
Obradovic, Z .
NATURE BIOTECHNOLOGY, 2001, 19 (09) :805-806
[96]  
Dunker AK, 2002, ADV PROTEIN CHEM, V62, P25
[97]   Intrinsic disorder and protein function [J].
Dunker, AK ;
Brown, CJ ;
Lawson, JD ;
Iakoucheva, LM ;
Obradovic, Z .
BIOCHEMISTRY, 2002, 41 (21) :6573-6582
[98]   Intrinsically disordered protein [J].
Dunker, AK ;
Lawson, JD ;
Brown, CJ ;
Williams, RM ;
Romero, P ;
Oh, JS ;
Oldfield, CJ ;
Campen, AM ;
Ratliff, CR ;
Hipps, KW ;
Ausio, J ;
Nissen, MS ;
Reeves, R ;
Kang, CH ;
Kissinger, CR ;
Bailey, RW ;
Griswold, MD ;
Chiu, M ;
Garner, EC ;
Obradovic, Z .
JOURNAL OF MOLECULAR GRAPHICS & MODELLING, 2001, 19 (01) :26-59
[99]   Laminins [J].
Durbeej, Madeleine .
CELL AND TISSUE RESEARCH, 2010, 339 (01) :259-268
[100]   Cracking the histone code: One, two, three methyls, you're out! [J].
Dutnall, RN .
MOLECULAR CELL, 2003, 12 (01) :3-4