Sequence Complexity of Amyloidogenic Regions in Intrinsically Disordered Human Proteins

被引：18

作者：

Das, Swagata ^{[1
]}

Pal, Uttam ^{[1
]}

Das, Supriya ^{[1
]}

Bagga, Khyati ^{[1
]}

Roy, Anupam ^{[1
]}

Mrigwani, Arpita ^{[1
]}

Maiti, Nakul C. ^{[1
]}

机构：

[1] Indian Inst Chem Biol, Council Sci & Ind Res, Struct Biol & Bioinformat Div, Kolkata, India

来源：

PLOS ONE | 2014年 / 9卷 / 03期

关键词：

MOLECULAR RECOGNITION FEATURES; FIBRIL-FORMING SEGMENTS; AGGREGATION-PRONE; ALPHA-SYNUCLEIN; UNSTRUCTURED PROTEINS; BINDING REGIONS; TAU-PROTEIN; WEB SERVER; PREDICTION; DETERMINANTS;

D O I：

10.1371/journal.pone.0089781

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：

An amyloidogenic region (AR) in a protein sequence plays a significant role in protein aggregation and amyloid formation. We have investigated the sequence complexity of AR that is present in intrinsically disordered human proteins. More than 80% human proteins in the disordered protein databases (DisProt+IDEAL) contained one or more ARs. With decrease of protein disorder, AR content in the protein sequence was decreased. A probability density distribution analysis and discrete analysis of AR sequences showed that similar to 8% residue in a protein sequence was in AR and the region was in average 8 residues long. The residues in the AR were high in sequence complexity and it seldom overlapped with low complexity regions (LCR), which was largely abundant in disorder proteins. The sequences in the AR showed mixed conformational adaptability towards alpha-helix, beta-sheet/strand and coil conformations.

引用

页数：19

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