지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2018.10
- 수록면
- 889 - 899 (11page)
- DOI
- 10.14348/molcells.2018.0192
이용수
초록· 키워드
오류제보하기
Intrinsically disordered proteins (IDPs) are highly unorthodox proteins that do not form three-dimensional structures under physiological conditions. The discovery of IDPs has destroyed the classical structure-function paradigm in protein science, 3-D structure = function, because IDPs even without well-folded 3-D structures are still capable of performing important biological functions and furthermore are associated with fatal diseases such as cancers, neurodegenerative diseases and viral pandemics. Pre-structured motifs (PreSMos) refer to transient local secondary structural elements present in the target-unbound state of IDPs. During the last two decades PreSMos have been steadily acknowledged as the critical determinants for target binding in dozens of IDPs. To date, the PreSMo concept provides the most convincing structural rationale explaining the IDP-target binding behavior at an atomic resolution. Here we present a brief developmental history of PreSMos and describe their common characteristics. We also provide a list of newly discovered PreSMos along with their functional relevance.
목차
등록된 정보가 없습니다.
참고문헌 (107)
참고문헌 신청
Andresen, C. / 2012 / Transient structure and dynamics in the disordered c-Myc transactivation domain affect Bin1 binding / Nucleic Acids Res. 40:6353~6366
Arai, M. / 2015 / Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding / Proc. Natl. Acad. Sci. USA 112:9614~9619
Atwal, R.S. / 2007 / Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity / Hum. Mol. Genet. 16:2600~2615
Baker, J.M. / 2007 / CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices / Nat. Struct. Mol. Biol. 14:738~745
Baldwin, R.L. / 2000 / Are denatured proteins ever random coils? / Proc Natl Acad Sci U S A 97:12391~12392
Arai, M. / 2015 / Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding / Proc. Natl. Acad. Sci. USA 112:9614~9619
Atwal, R.S. / 2007 / Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity / Hum. Mol. Genet. 16:2600~2615
Baker, J.M. / 2007 / CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices / Nat. Struct. Mol. Biol. 14:738~745
Baldwin, R.L. / 2000 / Are denatured proteins ever random coils? / Proc Natl Acad Sci U S A 97:12391~12392
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