The role of water molecules in the binding of class I and II peptides to the SH3 domain of the Fyn tyrosine kinase.

ABSTRACT: Interactions of proline-rich motifs with SH3 domains are present in signal transduction and other important cell processes. Analysis of structural and thermodynamic data suggest a relevant role of water molecules in these protein-protein interactions. To determine whether or not the SH3 domain of the Fyn tyrosine kinase shows the same behaviour, the crystal structures of its complexes with two high-affinity synthetic peptides, VSL12 and APP12, which are class I and II peptides, respectively, have been solved. In the class I complexes two water molecules were found at the binding interface that were not present in the class II complexes. The structures suggest a role of these water molecules in facilitating conformational changes in the SH3 domain to allow the binding of the class I or II p

SUBMITTER: Camara-Artigas A 

PROVIDER: S-EPMC5012211 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature