The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins.
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.
Potts
B C
BC
Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037, USA.
Smith
J
J
Akke
M
M
Macke
T J
TJ
Okazaki
K
K
Hidaka
H
H
Case
D A
DA
Chazin
W J
WJ
D000595:Amino Acid Sequence; D000818:Animals; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D018797:Cell Cycle Proteins; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D011817:Rabbits; D000075383:S100 Calcium Binding Protein A6; D009418:S100 Proteins; D017386:Sequence Homology, Amino Acid; D012996:Solutions
D002135:Calcium-Binding Proteins; D018797:Cell Cycle Proteins; D000075383:S100 Calcium Binding Protein A6; D009418:S100 Proteins; D012996:Solutions; C055351:S100A6 protein, human