Noncovalent complex between domain AB and domains CD*EF of parvalbumin.
The interaction between domain AB and domains CD*EF of pike parvalbumin III has been studied by intrinsic fluorescence spectroscopy. In the presence of Ca2+ ions, parvalbumin fragment 38-108 containing two calcium binding sites interacts with the short peptide 1-37 with association constant 10(5.3 +/- 0.5) M-1. Removal of Ca2+ ions results in the disappearance of the interaction. The affinity of the complex of the two fragments for calcium is 50-times higher than the affinity of the isolated fragment 38-108, but slightly lower than that of the intact protein.
Permyakov
E A
EA
Institute of Biological Physics, U.S.S.R. Academy of Sciences, Pushchino, Moscow region.
Medvedkin
V N
VN
Mitin
Y V
YV
Kretsinger
R H
RH
D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D004533:Egtazic Acid / Q000494:pharmacology; D006860:Hydrogen Bonding; D008958:Models, Molecular; D015394:Molecular Structure; D010320:Parvalbumins / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence
D010320:Parvalbumins; D004533:Egtazic Acid; D002118:Calcium