Journal of Proteomics & Bioinformatics
Open Access
ISSN: 0974-276X
ISSN: 0974-276X
Sangwook Wu, Hyun Jung Yoon, Sungmin Lee and Sun Joo Park
Pukyong National University, South Korea
Sungkyunkwan University, South Korea
Scientific Tracks Abstracts: J Proteomics Bioinform
Non-receptor tyrosine kinase c-Src plays a critical role in numerous cellular signaling pathways. Activation of c-Src involves a change from its inactive to the active state accompanied by large-scale conformational change depending on the phosphorylation state of two major phosphorylation sites, Tyr416 and Tyr527. A detailed mechanism for the entire conformational transition of c-Src via phosphorylation control of Tyr416 and Tyr527 is still elusive. In this study, we investigated the inactive to active conformational change of c-Src by targeted molecular dynamics simulation. Based on the simulation, we proposed a dynamical scenario for the activation process of c-Src. A detailed study of the conformational transition pathway based on network analysis suggests that Lys321 plays a key role in the c-Src activation process. Recent Publications 1. S Wu (2016) Loop-driven conformational transition between the alternative and collapsed form of prethrombin-2: targeted molecular dynamics study. Journal of Biomolecular Structure and Dynamics DOI:10.1080/07391102.2015.11 34347. 2. S Wu, C J Lee and L G Pedersen (2014) Analysis on long-range residueâ??residue communication using molecular dynamics. Proteins: Structure, Function and Bioinformatics 82:2896. 3. S Wu, W A Beard, L G Pedersen, and S Wilson (2014) Structural comparison of DNA polymerase architecture suggest a nucleotide gateway to the polymerase active site. Chemical Review 114:2759. 4. S Wu, J Tie, D W Stafford, and L G Pedersen (2014) Membrane topology for human vitamin K epoxide reductase (VKOR). Journal of Thrombosis and Haemostasis 12:112. 5. S Wu, S Liu, S Sim and L G Pedersen (2012) Weak antiferromagnetic coupling via a superexchange interaction between Mn (II)â??Mn (II) ions: A QM/MM study of the active site of human cytosolic X-propyl aminopeptidase P. Journal of Physical Chemistry Letter 3:2293.