Physical motif clustering within intrinsically disordered nucleoporin sequences reveals universal functional features.
Physical motif clustering within intrinsically disordered nucleoporin sequences reveals universal functional features.
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DOI:
10.1371/journal.pone.0073831
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发表时间:
2013
期刊:
影响因子:
3.7
通讯作者:
Gopinathan A
中科院分区:
文献类型:
--
作者:
Ando D;Colvin M;Rexach M;Gopinathan A
Bioinformatics of disordered proteins is especially challenging given high mutation rates for homologous proteins and that functionality may not be strongly related to sequence. Here we have performed a novel bioinformatic analysis, based on the spatial clustering of physically relevant features such as binding motifs and charges within disordered proteins, on thousands of Nuclear Pore Complex (NPC) FG motif containing proteins (FG nups). The biophysical mechanism by which FG nups regulate nucleocytoplasmic transport has remained elusive. Our analysis revealed a set of highly conserved spatial features in the sequence structure of individual FG nups, such as the separation, localization, and ordering of FG motifs and charged residues along the protein chain. These functionally conserved features provide insight into the particular biophysical mechanisms responsible for regulation of nucleocytoplasmic traffic in the NPC, strongly constraining current models. Additionally this method allows us to identify potentially functionally analogous disordered proteins across distantly related species.
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DOI:
10.1073/pnas.89.22.10915
发表时间:
1992-11-15
影响因子:
11.1
作者:
HENIKOFF, S;HENIKOFF, JG
通讯作者:
HENIKOFF, JG
影响因子:
4.3
作者:
Colwell LJ;Brenner MP;Ribbeck K
通讯作者:
Ribbeck K
DOI:
10.1074/mcp.m900038-mcp200
发表时间:
2009-09
期刊:
Molecular & cellular proteomics : MCP
影响因子:
--
作者:
DeGrasse JA;DuBois KN;Devos D;Siegel TN;Sali A;Field MC;Rout MP;Chait BT
通讯作者:
Chait BT
影响因子:
6.8
作者:
Eliezer, David
通讯作者:
Eliezer, David
影响因子:
7.5
作者:
Grunwald, David;Singer, Robert H.
通讯作者:
Singer, Robert H.