کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1931833 1050565 2010 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Solution structure of the N-terminal transactivation domain of ERM modified by SUMO-1
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Solution structure of the N-terminal transactivation domain of ERM modified by SUMO-1
چکیده انگلیسی

ERM is a member of the PEA3 group of the Ets transcription factor family that plays important roles in development and tumorigenesis. The PEA3s share an N-terminal transactivation domain (TADn) whose activity is inhibited by small ubiquitin-like modifier (SUMO). However, the consequences of sumoylation and its underlying molecular mechanism remain unclear. The domain structure of ERM TADn alone or modified by SUMO-1 was analyzed using small-angle X-ray scattering (SAXS). Low resolution shapes determined ab initio from the scattering data indicated an elongated shape and an unstructured conformation of TADn in solution. Covalent attachment of SUMO-1 does not perturb the structure of TADn as indicated by the linear arrangement of the SUMO moiety with respect to TADn. Thus, ERM belongs to the growing family of proteins that contain intrinsically unstructured regions. The flexible nature of TADn may be instrumental for ERM recognition and binding to diverse molecular partners.

Research highlights
► The N-terminal transactivation domain (TADn) of ERM is unstructured in solution.
► ERM belongs to the intrinsically disordered protein (IDP) family.
► Covalent attachment of SUMO-1 to TADn does not perturb the structural flexibility of TADn.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 399, Issue 1, 13 August 2010, Pages 104–110
نویسندگان
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