The STIL protein contains intrinsically disordered regions that mediate its protein-protein interactions

Hadar Amartely; Ahuvit David; Mario Lebendiker; Hadar Benyamini; Shai Izraeli; Assaf Friedler

doi:10.1039/c3cc45096a

The STIL protein contains intrinsically disordered regions that mediate its protein-protein interactions

Hadar Amartely, Ahuvit David, Mario Lebendiker, Hadar Benyamini, Shai Izraeli, Assaf Friedler

Institute of Chemistry

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

The STIL protein participates in mitosis and malignant transformation by regulating centrosomal duplication. Using biophysical methods we studied the structure and interactions of STIL. We revealed that its central domain is intrinsically disordered and mediates protein-protein interactions of STIL. The intrinsic disorder may provide STIL with the conformational flexibility required for its multitude binding.

Original language	English
Pages (from-to)	5245-5247
Number of pages	3
Journal	Chemical Communications
Volume	50
Issue number	40
DOIs	https://doi.org/10.1039/c3cc45096a
State	Published - 22 Apr 2014

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AU - David, Ahuvit

AU - Lebendiker, Mario

AU - Benyamini, Hadar

AU - Izraeli, Shai

AU - Friedler, Assaf

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AB - The STIL protein participates in mitosis and malignant transformation by regulating centrosomal duplication. Using biophysical methods we studied the structure and interactions of STIL. We revealed that its central domain is intrinsically disordered and mediates protein-protein interactions of STIL. The intrinsic disorder may provide STIL with the conformational flexibility required for its multitude binding.

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The STIL protein contains intrinsically disordered regions that mediate its protein-protein interactions

Abstract

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