MobiDB-lite 3.0: fast consensus annotation of intrinsic disorder flavors in proteins
MobiDB-lite 3.0: fast consensus annotation of intrinsic disorder flavors in proteins
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DOI：
10.1093/bioinformatics/btaa1045
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发表时间：
2020-12-01
期刊：
影响因子：
5.8
通讯作者：
Tosatto, Silvio C. E.
中科院分区：
文献类型：
--
作者：
Necci, Marco;Piovesan, Damiano;Tosatto, Silvio C. E.
动机：早期版本的PSDB-lite目前用于大规模蛋白质组注释平台，以检测内在疾病。然而，新的理论模型允许根据与特定聚合物性质或组成偏差相关的序列特征将固有无序区域分类为亚型。HDB-lite 3.0保持了其先前的速度和性能，但通过识别具有聚两性电解质、正或负聚电解质、低复杂性区域或富含半胱氨酸的特征的区域，脯氨酸或甘氨酸或极性残基。在人类蛋白质组的IDR中大量检测到亚区。新版本的SDB-lite代表了蛋白质组水平分析蛋白质紊乱的新步骤。
Motivation: The earlier version of MobiDB-lite is currently used in large-scale proteome annotation platforms to detect intrinsic disorder. However, new theoretical models allow for the classification of intrinsically disordered regions into subtypes from sequence features associated with specific polymeric properties or compositional bias.Results: MobiDB-lite 3.0 maintains its previous speed and performance but also provides a finer classification of disorder by identifying regions with characteristics of polyolyampholytes, positive or negative polyelectrolytes, low-complexity regions or enriched in cysteine, proline or glycine or polar residues. Subregions are abundantly detected in IDRs of the human proteome. The new version of MobiDB-lite represents a new step for the proteome level analysis of protein disorder.