Intermotif Communication Induces Hierarchical Ca(2+) Filling of Caldendrin
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Intermotif Communication Induces Hierarchical Ca(2+) Filling of Caldendrin. / Kiran, Uday; Regur, Phanindranath; Kreutz, Michael R; Sharma, Yogendra; Chakraborty, Asima.
in: BIOCHEMISTRY-US, Jahrgang 56, Nr. 19, 16.05.2017, S. 2467-2476.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Intermotif Communication Induces Hierarchical Ca(2+) Filling of Caldendrin
AU - Kiran, Uday
AU - Regur, Phanindranath
AU - Kreutz, Michael R
AU - Sharma, Yogendra
AU - Chakraborty, Asima
PY - 2017/5/16
Y1 - 2017/5/16
N2 - A crucial event in calcium signaling is the transition of a calcium sensor from the apo (Ca(2+) free) to the holo (Ca(2+)-saturated) state. Caldendrin (CDD) is a neuronal Ca(2+)-binding protein with two functional (EF3 and EF4) and two atypical (EF1 and EF2), non-Ca(2+)-binding EF-hand motifs. During the transition from the apo to the holo state, guided by the stepwise filling of Ca(2+), the protein passes through distinct states and acquires a stable conformational state when only EF3 is occupied by Ca(2+). This state is characterized by a Ca(2+)-derived structural gain in EF3 with destabilization of the EF4 motif. At higher Ca(2+) levels, when Ca(2+) fills in EF4, the motif regains stability. EF3 controls initial Ca(2+) binding and dictates structural destabilization of EF4. It is likely that this unexpected intermotif communication will have an impact on Ca(2+)-dependent target interactions.
AB - A crucial event in calcium signaling is the transition of a calcium sensor from the apo (Ca(2+) free) to the holo (Ca(2+)-saturated) state. Caldendrin (CDD) is a neuronal Ca(2+)-binding protein with two functional (EF3 and EF4) and two atypical (EF1 and EF2), non-Ca(2+)-binding EF-hand motifs. During the transition from the apo to the holo state, guided by the stepwise filling of Ca(2+), the protein passes through distinct states and acquires a stable conformational state when only EF3 is occupied by Ca(2+). This state is characterized by a Ca(2+)-derived structural gain in EF3 with destabilization of the EF4 motif. At higher Ca(2+) levels, when Ca(2+) fills in EF4, the motif regains stability. EF3 controls initial Ca(2+) binding and dictates structural destabilization of EF4. It is likely that this unexpected intermotif communication will have an impact on Ca(2+)-dependent target interactions.
KW - Amino Acid Motifs
KW - Amino Acid Substitution
KW - Animals
KW - Apoproteins
KW - Binding Sites
KW - Calcium Signaling
KW - Calcium-Binding Proteins
KW - Calorimetry
KW - Circular Dichroism
KW - Models, Molecular
KW - Mutagenesis, Site-Directed
KW - Mutation
KW - Nerve Tissue Proteins
KW - Protein Stability
KW - Protein Unfolding
KW - Rats
KW - Recombinant Proteins
KW - Spectrometry, Fluorescence
KW - Thermodynamics
KW - Titrimetry
KW - Comparative Study
KW - Journal Article
U2 - 10.1021/acs.biochem.7b00132
DO - 10.1021/acs.biochem.7b00132
M3 - SCORING: Journal article
C2 - 28437073
VL - 56
SP - 2467
EP - 2476
JO - BIOCHEMISTRY-US
JF - BIOCHEMISTRY-US
SN - 0006-2960
IS - 19
ER -