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PDBsum entry 1ypr
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Actin-binding protein
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PDB id
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1ypr
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure determination and characterization of saccharomyces cerevisiae profilin.
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Authors
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J.C.Eads,
N.M.Mahoney,
S.Vorobiev,
A.R.Bresnick,
K.K.Wen,
P.A.Rubenstein,
B.K.Haarer,
S.C.Almo.
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Ref.
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Biochemistry, 1998,
37,
11171-11181.
[DOI no: ]
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PubMed id
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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
percentage match of
0%.
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Abstract
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The structure of profilin from the budding yeast Saccharomyces cerevisiae has
been determined by X-ray crystallography at 2.3 A resolution. The overall fold
of yeast profilin is similar to the fold observed for other profilin structures.
The interactions of yeast and human platelet profilins with rabbit skeletal
muscle actin were characterized by titration microcalorimetry, fluorescence
titrations, and nucleotide exchange kinetics. The affinity of yeast profilin for
rabbit actin (2.9 microM) is approximately 30-fold weaker than the affinity of
human platelet profilin for rabbit actin (0.1 microM), and the relative
contributions of entropic and enthalpic terms to the overall free energy of
binding are different for the two profilins. The titration of pyrene-labeled
rabbit skeletal actin with human profilin yielded a Kd of 2.8 microM, similar to
the Kd of 2.0 microM for the interaction between yeast profilin and
pyrene-labeled yeast actin. The binding data are discussed in the context of the
known crystal structures of profilin and actin, and the residues present at the
actin-profilin interface. The affinity of yeast profilin for poly-L-proline was
determined from fluorescence measurements and is similar to the reported
affinity of Acanthamoeba profilin for poly-L-proline. Yeast profilin was shown
to catalyze adenine nucleotide exchange from yeast actin almost 2 orders of
magnitude less efficiently than human profilin and rabbit skeletal muscle actin.
The in vivo and in vitro properties of yeast profilin mutants with altered
poly-L-proline and actin binding sites are discussed in the context of the
crystal structure.
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