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

Tel Aviv University, The Hebrew University of Jerusalem

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

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

All Science Journal Classification (ASJC) codes

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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title = "The STIL protein contains intrinsically disordered regions that mediate its protein-protein interactions",

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.",

author = "Hadar Amartely and Ahuvit David and Mario Lebendiker and Hadar Benyamini and Shai Izraeli and Assaf Friedler",

year = "2014",

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T1 - The STIL protein contains intrinsically disordered regions that mediate its protein-protein interactions

AU - Amartely, Hadar

AU - David, Ahuvit

AU - Lebendiker, Mario

AU - Benyamini, Hadar

AU - Izraeli, Shai

AU - Friedler, Assaf

PY - 2014/4/22

Y1 - 2014/4/22

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=84892368963&partnerID=8YFLogxK

U2 - 10.1039/c3cc45096a

DO - 10.1039/c3cc45096a

M3 - مقالة

C2 - 24022511

SN - 1359-7345

VL - 50

SP - 5245

EP - 5247

JO - Chemical Communications

JF - Chemical Communications

IS - 40

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

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