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Oligomerization of the plasma membrane c ... ith different thermal stability
Oligomerization of the plasma membrane calcium pump involves two regions with different thermal stability
5378
Ca(2+) pump dimerization was studied by using a combined approach of thermal denaturation and fluorescence resonance energy transfer. The measurement of calcium pump ability to dimerize after the unfolding of individual functional domains of the enzyme demonstrated the existence of two different regions involved in the self-association process. One of these regions is highly susceptible to thermal unfolding and was identified as the calmodulin (CaM)-binding domain. The other region whose thermal stability is higher than those of the catalytic and CaM-binding domains could be related with the previously found C28W-binding regions.
Levi V, Rossi JP, Castello PR, González Flecha FL
FEBS letters
2000-10-20 00:00
483
2
99-103
Binding Sites,Calcium-Transporting ATPases,Calmodulin,Calmodulin-Binding Proteins,Dimerization,Erythrocyte Membrane,Fluorescence,Humans,Kinetics,Protein Binding,Protein Folding,Spectrometry, Fluorescence,Thermodynamics,Calmodulin,Calmodulin-Binding Proteins,Calcium-Transporting ATPases
Departamento de Química Biológica-IQUIFIB, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Junín 956, 1113 Buenos Aires, Argentina.
FEBS Lett.
0014-5793
S0014-5793(00)02093-7
0
False
11042261
