Biological Significance of Intrinsically Disordered Protein Structure

被引：0
|
作者：
Sato, Mamoru [1 ]
机构：
[1] Yokohama City Univ, Grad Sch Med Life Sci, Tsurumi Ku, 1-7-29 Suehiro Cho, Yokohama, Kanagawa 2300045, Japan
来源：
CHEM-BIO INFORMATICS JOURNAL | 2022年 / 22卷
关键词：
intrinsically disordered structure; intrinsically disordered protein (IDP); intrinsically disordered region (IDR); intracellular network; network hub protein; protein-protein interaction; novel target recognition; novel drug development;
D O I：
暂无
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Structural biology comprises "Structured biology" based on folded structure and "Unstructured biology" based on unfolded structure. Principal of "Unstructured biology" is intrinsically disordered protein (IDP), in which the polypeptide chain is highly disordered under physiological conditions. The length of the disordered polypeptide may extend to several hundred residues or more. Further, in protein comprising multiple domains, long disordered polypeptides exist between domains, even if each domain has a regularly folded structure. Such polypeptide region is called intrinsically disordered region (IDR). Several IDPs and IDRs exist in living cells and play important biological roles in intracellular networks. Here, the biological significance of IDP and IDR from various viewpoints are described. Overall, this review aims to encourage further studies on "Unstructured biology" based on unfolded/disordered protein structure.
引用
收藏
页码：26 / 37
页数：12
相关论文
共 50 条
  • [21] The Streptococcus phage protein paratox is an intrinsically disordered protein
    Asakereh, Iman
    Rutbeek, Nicole R.
    Singh, Manvir
    Davidson, David
    Prehna, Gerd
    Khajehpour, Mazdak
    PROTEIN SCIENCE, 2024, 33 (06)
  • [22] Probing hidden structure within intrinsically disordered protein domains with chiral mutagenesis
    Beckner, Ryan
    Zhou, Xiaoming
    Carter, Christien
    Gu, Jinge
    Valadez, Catherine
    McKnight, Steven
    Liszczak, Glen
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2024, 300 (03) : S753 - S754
  • [23] Assessing Intrinsically Disordered Protein Structure and Function through Carbon Detected NMR
    Showalter, Scott
    Sahu, Debashish
    Bastidas, Monique
    Lawrence, Chad
    FASEB JOURNAL, 2015, 29
  • [24] Effect of polyols on the structure and aggregation of recombinant human γ-Synuclein, an intrinsically disordered protein
    Roy, Sneha
    Bhat, Rajiv
    BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2018, 1866 (10): : 1029 - 1042
  • [25] Spectroscopic Characterization of Structure-Function Relationships in the Intrinsically Disordered Protein Complexin
    Snead, David
    Eliezer, David
    INTRINSICALLY DISORDERED PROTEINS, 2018, 611 : 227 - 286
  • [26] Calcium ions modulate the structure of the intrinsically disordered Nucleobindin-2 protein
    Skorupska, Anna
    Bystranowska, Dominika
    Dabrowska, Katarzyna
    Ozyhar, Andrzej
    INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2020, 154 : 1091 - 1104
  • [27] Mutational scan inferred binding energetics and structure in intrinsically disordered protein CcdA
    Chandra, Soumyanetra
    Manjunath, Kavyashree
    Asok, Aparna
    Varadarajan, Raghavan
    PROTEIN SCIENCE, 2023, 32 (03)
  • [28] The Functional Significance of Intrinsically Disordered Protein Regions Encoded by the Diabetes Gene Clec16A
    Gingerich, Morgan
    Liu, Xueying
    Vincent, Michael
    Chai, Bioxian
    Vozheiko, Tracy
    Pearson, Gemma
    Klionsky, Daniel
    Schenll, Santiago
    Scott, Soleimanpour
    BIOPHYSICAL JOURNAL, 2019, 116 (03) : 203A - 203A
  • [29] Adding intrinsically disordered proteins to biological ageing clocks
    Dormann, Dorothee
    Lemke, Edward Anton
    NATURE CELL BIOLOGY, 2024, 26 (06) : 851 - 858
  • [30] A Substantial Improvement in Predictions of Intrinsically Disordered Protein
    Williams, Robert W.
    BIOPHYSICAL JOURNAL, 2015, 108 (02) : 229A - 229A
12345