Diversity and structural-functional insights of alpha-solenoid proteins.

IF 4.5 3区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Protein Science Pub Date : 2024-11-01 DOI:10.1002/pro.5189
Paula Nazarena Arrías, Zarifa Osmanli, Estefanía Peralta, Patricio Manuel Chinestrad, Alexander Miguel Monzon, Silvio C E Tosatto
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引用次数: 0

Abstract

Alpha-solenoids are a significant and diverse subset of structured tandem repeat proteins (STRPs) that are important in various domains of life. This review examines their structural and functional diversity and highlights their role in critical cellular processes such as signaling, apoptosis, and transcriptional regulation. Alpha-solenoids can be classified into three geometric folds: low curvature, high curvature, and corkscrew, as well as eight subfolds: ankyrin repeats; Huntingtin, elongation factor 3, protein phosphatase 2A, and target of rapamycin; armadillo repeats; tetratricopeptide repeats; pentatricopeptide repeats; Pumilio repeats; transcription activator-like; and Sel-1 and Sel-1-like repeats. These subfolds represent distinct protein families with unique structural properties and functions, highlighting the versatility of alpha-solenoids. The review also discusses their association with disease, highlighting their potential as therapeutic targets and their role in protein design. Advances in state-of-the-art structure prediction methods provide new opportunities and challenges in the functional characterization and classification of this kind of fold, emphasizing the need for continued development of methods for their identification and proper data curation and deposition in the main databases.

α-类烯醇蛋白的多样性和结构功能见解。
α-solenoids是结构串联重复蛋白(STRPs)的一个重要且多样化的亚群,在生命的各个领域都很重要。本综述探讨了它们在结构和功能上的多样性,并重点介绍了它们在信号传导、细胞凋亡和转录调控等关键细胞过程中的作用。α-solenoids可分为三种几何褶皱:低曲率、高曲率和开瓶器褶皱,以及八个亚褶皱:ankyrin重复序列;Huntingtin、伸长因子3、蛋白磷酸酶2A和雷帕霉素靶标;犰狳重复序列;四三肽重复序列;五三肽重复序列;Pumilio重复序列;类转录激活因子;以及Sel-1和Sel-1-like重复序列。这些亚结构代表了不同的蛋白质家族,具有独特的结构特性和功能,突显了α-亚磺酸的多样性。综述还讨论了它们与疾病的关系,强调了它们作为治疗靶点的潜力及其在蛋白质设计中的作用。最先进的结构预测方法的进步为这类折叠的功能表征和分类提供了新的机遇和挑战,强调了继续开发其识别方法以及适当的数据整理和存入主要数据库的必要性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Protein Science
Protein Science 生物-生化与分子生物学
CiteScore
12.40
自引率
1.20%
发文量
246
审稿时长
1 months
期刊介绍: Protein Science, the flagship journal of The Protein Society, is a publication that focuses on advancing fundamental knowledge in the field of protein molecules. The journal welcomes original reports and review articles that contribute to our understanding of protein function, structure, folding, design, and evolution. Additionally, Protein Science encourages papers that explore the applications of protein science in various areas such as therapeutics, protein-based biomaterials, bionanotechnology, synthetic biology, and bioelectronics. The journal accepts manuscript submissions in any suitable format for review, with the requirement of converting the manuscript to journal-style format only upon acceptance for publication. Protein Science is indexed and abstracted in numerous databases, including the Agricultural & Environmental Science Database (ProQuest), Biological Science Database (ProQuest), CAS: Chemical Abstracts Service (ACS), Embase (Elsevier), Health & Medical Collection (ProQuest), Health Research Premium Collection (ProQuest), Materials Science & Engineering Database (ProQuest), MEDLINE/PubMed (NLM), Natural Science Collection (ProQuest), and SciTech Premium Collection (ProQuest).
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