 |
PDBsum entry 2prf
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Actin-binding
|
PDB id
|
|
|
|
2prf
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
J Cell Biol
122:1277-1283
(1993)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Three-dimensional solution structure of Acanthamoeba profilin-I.
|
|
V.K.Vinson,
S.J.Archer,
E.E.Lattman,
T.D.Pollard,
D.A.Torchia.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
We have determined a medium resolution three-dimensional solution structure of
Acanthamoeba profilin-I by multidimensional nuclear magnetic resonance
spectroscopy. This 13-kD actin binding protein consists of a five stranded
antiparallel beta sheet flanked by NH2- and COOH-terminal helices on one face
and by a third helix and a two stranded beta sheet on the other face. Data from
actin-profilin cross-linking experiments and the localization of conserved
residues between profilins in different phyla indicate that actin binding occurs
on the molecular face occupied by the terminal helices. The other face of the
molecule contains the residues that differ between Acanthamoeba profilins-I and
II and may be important in determining the difference in polyphosphoinositide
binding between these isoforms. This suggests that lipids and actin bind to
different faces of the molecule.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
S.Morales,
J.C.Jiménez-López,
A.J.Castro,
M.I.Rodríguez-García,
and
J.D.Alché
(2008).
Olive pollen profilin (Ole e 2 allergen) co-localizes with highly active areas of the actin cytoskeleton and is released to the culture medium during in vitro pollen germination.
|
| |
J Microsc,
231,
332-341.
|
|
|
|
|
|
|
L.J.Ball,
R.Kühne,
J.Schneider-Mergener,
and
H.Oschkinat
(2005).
Recognition of Proline-Rich Motifs by Protein-Protein-Interaction Domains.
|
| |
Angew Chem Int Ed Engl,
44,
2852-2869.
|
|
|
|
|
|
|
S.J.Winder
(2003).
Structural insights into actin-binding, branching and bundling proteins.
|
| |
Curr Opin Cell Biol,
15,
14-22.
|
|
|
|
|
|
|
J.Lu,
and
T.D.Pollard
(2001).
Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast.
|
| |
Mol Biol Cell,
12,
1161-1175.
|
|
|
|
|
|
|
D.B.Ostrander,
E.G.Ernst,
T.B.Lavoie,
and
J.A.Gorman
(1999).
Polyproline binding is an essential function of human profilin in yeast.
|
| |
Eur J Biochem,
262,
26-35.
|
|
|
|
|
|
|
M.R.Holbrook,
J.B.O'Donnell,
L.L.Slakey,
and
D.J.Gross
(1999).
Epidermal growth factor receptor internalization rate is regulated by negative charges near the SH2 binding site Tyr992.
|
| |
Biochemistry,
38,
9348-9356.
|
|
|
|
|
|
|
M.Van Troys,
J.Vandekerckhove,
and
C.Ampe
(1999).
Structural modules in actin-binding proteins: towards a new classification.
|
| |
Biochim Biophys Acta,
1448,
323-348.
|
|
|
|
|
|
|
A.Ledesma,
R.Rodríguez,
and
M.Villalba
(1998).
Olive-pollen profilin. Molecular and immunologic properties.
|
| |
Allergy,
53,
520-526.
|
|
|
|
|
|
|
E.Korenbaum,
P.Nordberg,
C.Björkegren-Sjögren,
C.E.Schutt,
U.Lindberg,
and
R.Karlsson
(1998).
The role of profilin in actin polymerization and nucleotide exchange.
|
| |
Biochemistry,
37,
9274-9283.
|
|
|
|
|
|
|
N.M.Mahoney,
and
S.C.Almo
(1998).
Crystallization and preliminary X-ray analysis of human platelet profilin complexed with an oligo proline peptide.
|
| |
Acta Crystallogr D Biol Crystallogr,
54,
108-110.
|
|
|
|
|
|
|
A.A.Fedorov,
T.Ball,
N.M.Mahoney,
R.Valenta,
and
S.C.Almo
(1997).
The molecular basis for allergen cross-reactivity: crystal structure and IgE-epitope mapping of birch pollen profilin.
|
| |
Structure,
5,
33-45.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
K.S.Thorn,
H.E.Christensen,
R.Shigeta,
D.Huddler,
L.Shalaby,
U.Lindberg,
N.H.Chua,
and
C.E.Schutt
(1997).
The crystal structure of a major allergen from plants.
|
| |
Structure,
5,
19-32.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
K.Schlüter,
B.M.Jockusch,
and
M.Rothkegel
(1997).
Profilins as regulators of actin dynamics.
|
| |
Biochim Biophys Acta,
1359,
97.
|
|
|
|
|
|
|
L.Vidali,
and
P.K.Hepler
(1997).
Characterization and localization of profilin in pollen grains and tubes of Lilium longiflorum.
|
| |
Cell Motil Cytoskeleton,
36,
323-338.
|
|
|
|
|
|
|
A.Tarachandani,
and
Y.L.Wang
(1996).
Site-directed mutagenesis enabled preparation of a functional fluorescent analog of profilin: biochemical characterization and localization in living cells.
|
| |
Cell Motil Cytoskeleton,
34,
313-323.
|
|
|
|
|
|
|
E.C.Petrella,
L.M.Machesky,
D.A.Kaiser,
and
T.D.Pollard
(1996).
Structural requirements and thermodynamics of the interaction of proline peptides with profilin.
|
| |
Biochemistry,
35,
16535-16543.
|
|
|
|
|
|
|
I.Karakesisoglou,
M.Schleicher,
B.C.Gibbon,
and
C.J.Staiger
(1996).
Plant profilins rescue the aberrant phenotype of profilin-deficient Dictyostelium cells.
|
| |
Cell Motil Cytoskeleton,
34,
36-47.
|
|
|
|
|
|
|
M.K.Balasubramanian,
A.Feoktistova,
D.McCollum,
and
K.L.Gould
(1996).
Fission yeast Sop2p: a novel and evolutionarily conserved protein that interacts with Arp3p and modulates profilin function.
|
| |
EMBO J,
15,
6426-6437.
|
|
|
|
|
|
|
A.Lambrechts,
J.van Damme,
M.Goethals,
J.Vandekerckhove,
and
C.Ampe
(1995).
Purification and characterization of bovine profilin II. Actin, poly(L-proline) and inositolphospholipid binding.
|
| |
Eur J Biochem,
230,
281-286.
|
|
|
|
|
|
|
H.Q.Sun,
K.Kwiatkowska,
and
H.L.Yin
(1995).
Actin monomer binding proteins.
|
| |
Curr Opin Cell Biol,
7,
102-110.
|
|
|
|
|
|
|
W.J.Metzler,
B.T.Farmer,
K.L.Constantine,
M.S.Friedrichs,
T.Lavoie,
and
L.Mueller
(1995).
Refined solution structure of human profilin I.
|
| |
Protein Sci,
4,
450-459.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
A.A.Fedorov,
K.A.Magnus,
M.H.Graupe,
E.E.Lattman,
T.D.Pollard,
and
S.C.Almo
(1994).
X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates.
|
| |
Proc Natl Acad Sci U S A,
91,
8636-8640.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
E.H.Egelman
(1994).
Actin filament structure. The ghost of ribbons past.
|
| |
Curr Biol,
4,
79-81.
|
|
|
|
|
|
|
K.Giehl,
R.Valenta,
M.Rothkegel,
M.Ronsiek,
H.G.Mannherz,
and
B.M.Jockusch
(1994).
Interaction of plant profilin with mammalian actin.
|
| |
Eur J Biochem,
226,
681-689.
|
|
|
|
|
|
|
M.A.Markus,
T.Nakayama,
P.Matsudaira,
and
G.Wagner
(1994).
1H, 15N, 13C and 13CO resonance assignments and secondary structure of villin 14T, a domain conserved among actin-severing proteins.
|
| |
J Biomol NMR,
4,
553-574.
|
|
|
|
|
|
|
M.D.Rozycki,
J.C.Myslik,
C.E.Schutt,
and
U.Lindberg
(1994).
Structural aspects of actin-binding proteins.
|
| |
Curr Opin Cell Biol,
6,
87-95.
|
|
|
|
|
|
|
M.K.Balasubramanian,
B.R.Hirani,
J.D.Burke,
and
K.L.Gould
(1994).
The Schizosaccharomyces pombe cdc3+ gene encodes a profilin essential for cytokinesis.
|
| |
J Cell Biol,
125,
1289-1301.
|
|
|
|
|
|
|
R.H.Sohn,
and
P.J.Goldschmidt-Clermont
(1994).
Profilin: at the crossroads of signal transduction and the actin cytoskeleton.
|
| |
Bioessays,
16,
465-472.
|
|
|
|
|
|
|
B.K.Haarer,
A.S.Petzold,
and
S.S.Brown
(1993).
Mutational analysis of yeast profilin.
|
| |
Mol Cell Biol,
13,
7864-7873.
|
|
|
|
|
|
|
J.A.Theriot,
and
T.J.Mitchison
(1993).
The three faces of profilin.
|
| |
Cell,
75,
835-838.
|
|
|
|
|
|
|
L.M.Machesky,
and
T.D.Poland
(1993).
Profilin as a potential mediator of membrane-cytoskeleton communication.
|
| |
Trends Cell Biol,
3,
381-385.
|
|
|
|
|
|
|
M.Way,
and
P.Matsudaira
(1993).
The secrets of severing?
|
| |
Curr Biol,
3,
887-890.
|
|
|
|
|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
|
|
Links
