دورية أكاديمية
أعرض في EDS

Expanding the Range of Protein Function at the Far End of the Order-Structure Continuum.

التفاصيل البيبلوغرافية
العنوان: Expanding the Range of Protein Function at the Far End of the Order-Structure Continuum.
المؤلفون: Burger VM; From the Research Laboratory for Electronics, Department of Electrical Engineering & Computer Science, and., Nolasco DO; From the Research Laboratory for Electronics, Department of Electrical Engineering & Computer Science, and., Stultz CM; From the Research Laboratory for Electronics, Department of Electrical Engineering & Computer Science, and the Institute for Medical Engineering and Science, Massachusetts Institute of Technology, Cambridge, Massachusetts 02138 cmstultz@mit.edu.
المصدر: The Journal of biological chemistry [J Biol Chem] 2016 Mar 25; Vol. 291 (13), pp. 6706-13. Date of Electronic Publication: 2016 Feb 05.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't; Review
اللغة: English
بيانات الدورية: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
أسماء مطبوعة: Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
مواضيع طبية MeSH: Amino Acids/*chemistry , CREB-Binding Protein/*chemistry , Colicins/*chemistry , Eukaryotic Initiation Factors/*chemistry , Intrinsically Disordered Proteins/*chemistry, Amino Acid Sequence ; Amino Acids/metabolism ; CREB-Binding Protein/genetics ; CREB-Binding Protein/metabolism ; Colicins/genetics ; Colicins/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Eukaryotic Initiation Factors/genetics ; Eukaryotic Initiation Factors/metabolism ; Humans ; Intrinsically Disordered Proteins/genetics ; Intrinsically Disordered Proteins/metabolism ; Protein Binding ; Protein Folding ; Protein Interaction Domains and Motifs ; Protein Structure, Secondary ; Structure-Activity Relationship ; Thermodynamics
مستخلص: The traditional view of the structure-function paradigm is that a protein's function is inextricably linked to a well defined, three-dimensional structure, which is determined by the protein's primary amino acid sequence. However, it is now accepted that a number of proteins do not adopt a unique tertiary structure in solution and that some degree of disorder is required for many proteins to perform their prescribed functions. In this review, we highlight how a number of protein functions are facilitated by intrinsic disorder and introduce a new protein structure taxonomy that is based on quantifiable metrics of a protein's disorder.
(© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.)
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فهرسة مساهمة: Keywords: biophysics; conformational change; intrinsically disordered protein; protein folding; protein structure
سلسلة جزيئية: PDB 1bh4; 1jjs; 1k7b; 1kbh; 1qjp; 1ujw; 1zoq; 2c52; 2ivz; 2k3g; 2k3j; 2kac; 2kkj; 2l14; 2mx4; 3O0e; 3am7
المشرفين على المادة: 0 (Amino Acids)
0 (Colicins)
0 (EIF4EBP2 protein, human)
0 (Eukaryotic Initiation Factors)
0 (Intrinsically Disordered Proteins)
0 (immE9 protein, E coli)
EC 2.3.1.48 (CREB-Binding Protein)
EC 2.3.1.48 (CREBBP protein, human)
تواريخ الأحداث: Date Created: 20160207 Date Completed: 20160805 Latest Revision: 20240325
رمز التحديث: 20240325
مُعرف محوري في PubMed: PMC4807258
DOI: 10.1074/jbc.R115.692590
PMID: 26851282
قاعدة البيانات: MEDLINE
الوصف
تدمد:1083-351X
DOI:10.1074/jbc.R115.692590