Structural Analysis of FGFR1 Kinase Activation through Molecular Dynamics Simulation

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CSB
2004
2004 IEEE Computational Systems Bioinformatics Conference (CSB'04)
Abstract - Structural Analysis of FGFR1 Kinase Activation through Molecular Dynamics Simulation

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2004 IEEE Computational Systems Bioinformatics Conference (CSB'04)

Structural Analysis of FGFR1 Kinase Activation through Molecular Dynamics Simulation (PDF)

Stanford, California

August 16-August 19

ISBN: 0-7695-2194-0

	ASCII Text	x
	Peng Wang, Zhengchang Su, Juntao Guo, Ying Xu, "Structural Analysis of FGFR1 Kinase Activation through Molecular Dynamics Simulation," Computational Systems Bioinformatics Conference, International IEEE Computer Society, pp. 700-701, 2004 IEEE Computational Systems Bioinformatics Conference (CSB'04), 2004.

	BibTex	x
	@article{ 10.1109/CSB.2004.1332550, author = {Peng Wang and Zhengchang Su and Juntao Guo and Ying Xu}, title = {Structural Analysis of FGFR1 Kinase Activation through Molecular Dynamics Simulation}, journal ={Computational Systems Bioinformatics Conference, International IEEE Computer Society}, volume = {0}, year = {2004}, isbn = {0-7695-2194-0}, pages = {700-701}, doi = {http://doi.ieeecomputersociety.org/10.1109/CSB.2004.1332550}, publisher = {IEEE Computer Society}, address = {Los Alamitos, CA, USA}, }

	RefWorks Procite/RefMan/Endnote	x
	TY - CONF JO - Computational Systems Bioinformatics Conference, International IEEE Computer Society TI - Structural Analysis of FGFR1 Kinase Activation through Molecular Dynamics Simulation SN - 0-7695-2194-0 SP700 EP701 A1 - Peng Wang, A1 - Zhengchang Su, A1 - Juntao Guo, A1 - Ying Xu, PY - 2004 KW - null VL - 0 JA - Computational Systems Bioinformatics Conference, International IEEE Computer Society ER -

Peng Wang, University of Georgia

Zhengchang Su, University of Georgia

Juntao Guo, University of Georgia

Ying Xu, University of Georgia

DOI Bookmark: http://doi.ieeecomputersociety.org/10.1109/CSB.2004.1332550

Receptor tyrokine kinases are critical regulators of signal transduction pathways mediating cellular homeostasis. Enhanced kinase activities via mutation and other genetic alternations have been observed in many human cancers. We performed a 4 ns molecular dynamics (MD) simulation of the kinase domain of fibroblast growth factor receptor 1 (FGFR1) to study the mechanism that controls its activation. Our simulation revealed the key atomic events that allow substrate access and kinase activation. This dynamic information will facilitate the design of new inhibitors for use in the treatment of cancer.

Citation:

Peng Wang, Zhengchang Su, Juntao Guo, Ying Xu, "Structural Analysis of FGFR1 Kinase Activation through Molecular Dynamics Simulation," csb, pp.700-701, 2004 IEEE Computational Systems Bioinformatics Conference (CSB'04), 2004

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