 |
|
Title
|
|
The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins.
|
|
|
Authors
|
|
B.C.Potts,
J.Smith,
M.Akke,
T.J.Macke,
K.Okazaki,
H.Hidaka,
D.A.Case,
W.J.Chazin.
|
|
|
Ref.
|
|
Nat Struct Biol, 1995,
2,
790-796.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The S100 calcium-binding proteins are implicated as effectors in
calcium-mediated signal transduction pathways. The three-dimensional structure
of the S100 protein calcyclin has been determined in solution in the apo state
by NMR spectroscopy and a computational strategy that incorporates a systematic
docking protocol. This structure reveals a symmetric homodimeric fold that is
unique among calcium-binding proteins. Dimerization is mediated by hydrophobic
contacts from several highly conserved residues, which suggests that the dimer
fold identified for calcyclin will serve as a structural paradigm for the S100
subfamily of calcium-binding proteins.
|
|
|
|