Focal Adhesion Kinase as a Cellular Mechano-Sensor

Jing Zhou, Agnieszka Bronowska, Bogdan Costescu and Frauke Graeter ()
Additional contact information
Jing Zhou: Heidelberg Institute for Theoretical Studies
Agnieszka Bronowska: Heidelberg Institute for Theoretical Studies
Bogdan Costescu: Heidelberg Institute for Theoretical Studies
Frauke Graeter: Heidelberg Institute for Theoretical Studies

A chapter in High Performance Computing in Science and Engineering ‘13, 2013, pp 663-669 from Springer

Abstract: Abstract Focal adhesion kinase (FAK) is a component of focal adhesion sites, which plays a crucial role in cell differentiation and motility. Using molecular dynamic simulations, we observed that binding of the phospho-inositide phosphatidylinositol-4,5-bisphosphate ( $$\mathit{PIP}_{2}$$ ) by FAK can induce major conformational changes of FAK and exposure of its auto-phosphorylation site, but it cannot induce FAK’s activation. Our results support the biological experimental data by providing an atomic description of FAK’s conformational changes within FERM and kinase domains.

Keywords: Molecular Dynamics Simulation; Focal Adhesion Kinase; Kinase Domain; Focal Adhesion Kinase Activation; Ferm Domain (search for similar items in EconPapers)
Date: 2013
References: Add references at CitEc
Citations:

There are no downloads for this item, see the EconPapers FAQ for hints about obtaining it.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:spr:sprchp:978-3-319-02165-2_46

Ordering information: This item can be ordered from
http://www.springer.com/9783319021652

DOI: 10.1007/978-3-319-02165-2_46

Access Statistics for this chapter

More chapters in Springer Books from Springer
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().