Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: Hepatitis C virus NS5A protein binds the SH3 domain of the Fyn tyrosine kinase with high affinity: mutagenic analysis of residues within the SH3 domain that | Virology Journal BioMed Central Research Hepatitis C virus NS5A protein binds the SH3 domain of the Fyn tyrosine kinase with high affinity mutagenic analysis of residues within the SH3 domain that contribute to the interaction Holly Shelton1 2 and Mark Harris 1 Address institute of Molecular and Cellular Biology Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology University of Leeds Leeds LS2 9JT UK and 2Department of Microbiology School of Biological Sciences The University of Reading Whiteknights RG6 6AJ Reading UK Email Holly Shelton - Mark Harris - Corresponding author Open Access Published II February 2008 Received 8 January 2008 Accepted 11 February 2008 Virology journal 2008 5 24 doi 1743-422X-5-24 This article is available from http content 5 1 24 2008 Shelton and Harris licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background The hepatitis C virus HCV non-structural 5A protein NS5A contains a highly conserved C-terminal polyproline motif with the consensus sequence Pro-X-X-Pro-X-Arg that is able to interact with the Src-homology 3 SH3 domains of a variety of cellular proteins. Results To understand this interaction in more detail we have expressed two N-terminally truncated forms of NS5A in E. coli and examined their interactions with the SH3 domain of the Src-family tyrosine kinase Fyn. Surface plasmon resonance analysis revealed that NS5A binds to the Fyn SH3 domain with what can be considered a high affinity SH3 domain-ligand interaction 629 nM and this binding did not require the presence of domain I of NS5A amino acid residues 32-250 . Mutagenic analysis of the Fyn SH3 domain demonstrated the .
