|
Figure 2.
Structure of the PCSK9-EGF-A complex. The sigmaA weighted
2F[o] - F[c] electron density map contoured at 1σ shows the
conformational change that occurs upon protonation of His-306.
EGF-A and PCSK9 are represented as a stick model. Residues
involved in the pH-dependent conformational change are colored
according to element type as follows: nitrogen, blue; oxygen,
red; EGF-A carbon, yellow; PCSK9 carbon, green. All other
residues are colored gray. A, at acidic pH, His-306 of EGF-A
forms a salt bridge with Asp-374 of PCSK9. B, at neutral pH,
His-306 of EGF-A forms an intramolecular hydrogen bond with
Ser-305. C, FH mutation H306Y of EGF-A is able to form a
hydrogen bond with Asp-374 of PCSK9 at neutral pH.
|
