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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2020.1
- 수록면
- 899 - 908 (10page)
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초록· 키워드
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Intrinsically disordered proteins or regions (IDPs or IDRs) are widespread in the eukaryotic proteome. Although lacking stable three-dimensional structures in the free forms, IDRs perform critical functions in various cellular processes. Accordingly, mutations and altered expression of IDRs are associated with many pathological conditions. Hence, it is of great importance to understand at the molecular level how IDRs interact with their binding partners. In particular, discovering the unique interaction features of IDRs originating from their dynamic nature may reveal uncharted regulatory mechanisms of specific biological processes. Here we discuss the mechanisms of the macromolecular interactions mediated by IDRs and present the relevant cellular processes including transcription, cell cycle progression, signaling, and nucleocytoplasmic transport. Of special interest is the multivalent binding nature of IDRs driving assembly of multicomponent macromolecular complexes. Integrating the previous theoretical and experimental investigations, we suggest that such IDR-driven multiprotein complexes can function as versatile allosteric switches to process diverse cellular signals. Finally, we discuss the future challenges and potential medical applications of the IDR research.
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참고문헌 (93)
참고문헌 신청
Anfinsen, C. B. / 1961 / The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain / Proc. Natl. Acad. Sci. U. S. A 47:1309~1314
Babu, M. M. / 2011 / Intrinsically disordered proteins : regulation and disease / Curr. Opin. Struct. Biol 21:432~440
Baker, J. M. / 2007 / CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices / Nat. Struct. Mol. Biol 14:738~745
Blus, B. J. / 2019 / Allosteric modulation of nucleoporin assemblies by intrinsically disordered regions / Sci. Adv. 5:eaax1836
Borcherds, W. / 2014 / Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells / Nat. Chem. Biol 10:1000~1002
Babu, M. M. / 2011 / Intrinsically disordered proteins : regulation and disease / Curr. Opin. Struct. Biol 21:432~440
Baker, J. M. / 2007 / CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices / Nat. Struct. Mol. Biol 14:738~745
Blus, B. J. / 2019 / Allosteric modulation of nucleoporin assemblies by intrinsically disordered regions / Sci. Adv. 5:eaax1836
Borcherds, W. / 2014 / Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells / Nat. Chem. Biol 10:1000~1002
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