 |
PDBsum entry 1acf
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Contractile protein
|
PDB id
|
|
|
|
1acf
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
X-Ray structures of isoforms of the actin-Binding protein profilin that differ in their affinity for phosphatidylinositol phosphates.
|
 |
|
Authors
|
 |
A.A.Fedorov,
K.A.Magnus,
M.H.Graupe,
E.E.Lattman,
T.D.Pollard,
S.C.Almo.
|
 |
|
Ref.
|
 |
Proc Natl Acad Sci U S A, 1994,
91,
8636-8640.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
|
Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
|
 |
 |
|
Abstract
|
 |
|
We determined the structures of Acanthamoeba profilin I and profilin II by x-ray
crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide
folds and the actin-binding surfaces of the amoeba profilins are very similar to
those of bovine and human profilins. The electrostatic potential surfaces of the
two Acanthamoeba isoforms differ. Two areas of high positive potential on the
surface of profilin II are candidate binding sites for phosphatidylinositol
phosphates. The proximity of these sites to the actin binding site provides an
explanation for the competition between actin and lipids for binding profilin.
|
 |
|
|
|
|
 |