Title : The promiscuous binding of the Fyn SH3 domain to a peptide from the NS5A protein.

Pub. Date : 2012 Aug

PMID : 22868769






3 Functional Relationships(s)
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1 The 1.5 A resolution crystal structure of a complex between the SH3 domain of the Fyn tyrosine kinase and the C-terminal proline-rich motif of the NS5A-derived peptide APPIPPPRRKR has been solved. Proline FYN proto-oncogene, Src family tyrosine kinase Homo sapiens
2 The proline-rich motif present in the NS5A protein seems to be important for RNA replication and virus assembly, and the promiscuous interaction of the Fyn SH3 domain with the NS5A C-terminal proline-rich peptide found in this crystallographic structure may be important in the virus infection cycle. Proline FYN proto-oncogene, Src family tyrosine kinase Homo sapiens
3 The proline-rich motif present in the NS5A protein seems to be important for RNA replication and virus assembly, and the promiscuous interaction of the Fyn SH3 domain with the NS5A C-terminal proline-rich peptide found in this crystallographic structure may be important in the virus infection cycle. Proline FYN proto-oncogene, Src family tyrosine kinase Homo sapiens