ABCC8 p.Phe221Ala
[switch to full view]Comments [show]
None has been submitted yet.
PMID: 18547145
[PubMed]
Olivares-Illana V et al: "Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus."
No.
Sentence
Comment
105
The (F221A) mutation was introduced in the CapACt segment of the chimeric CapAB protein in order to verify the essential role of residue F221a suggested by the structure.
X
ABCC8 p.Phe221Ala 18547145:105:5
status: NEW106 A strongly decreased autokinase activity was observed with the CapAB(F221A) mutant compared to the wild-type CapAB protein (Figure S2).
X
ABCC8 p.Phe221Ala 18547145:106:69
status: NEW107 Preliminary fluorescence experiments using labelled nucleotide analogs further confirmed that this loss of activity is correlated with a reduced affinity of the CapAB(F221A) mutant for the nucleotide (unpublished data).
X
ABCC8 p.Phe221Ala 18547145:107:167
status: NEW273 Functional Analysis of the CapA Residue F221a The autophosphorylation activity of the CapAB chimeric protein (WT) and of the F221 mutated form (F221A) was analyzed by SDS-PAGE and autoradiography.
X
ABCC8 p.Phe221Ala 18547145:273:144
status: NEW