Inositol polyphosphate 5-phosphatase OCRL: Difference between revisions

The N591K mutation also causes significant reduction in binding of Rab8a protein but the reason for this is different than in the case of F668V mutation. This AA is not part of any binding site but it seems to be important in the maintenance of the correct features of the ASH domain which are essential for the Rab8a binding. The effect of this mutation was studied in silico and the study showed that the mutation caused the ASH domain to alter its flexibility and overall fold. Although the most significant change was observed in the AAs that surrounded the N591K mutation, the substitution caused subsequent changes in most parts of the protein which brought about decreases of prevalence of hydrogen bonds between Rab8a and OCRL1 which led to a lower stability of their interaction.<ref name="com"/>

[[3D structures of inositol polyphosphate 5-phosphatase OCRL]]