Research ExplorerPublicationsIntermotif Communication Induces Hierarchical Ca(2+) Filling...

Intermotif Communication Induces Hierarchical Ca(2+) Filling of Caldendrin

Standard

Intermotif Communication Induces Hierarchical Ca(2+) Filling of Caldendrin. / Kiran, Uday; Regur, Phanindranath; Kreutz, Michael R; Sharma, Yogendra; Chakraborty, Asima.

In: BIOCHEMISTRY-US, Vol. 56, No. 19, 16.05.2017, p. 2467-2476.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Kiran, U, Regur, P, Kreutz, MR, Sharma, Y & Chakraborty, A 2017, 'Intermotif Communication Induces Hierarchical Ca(2+) Filling of Caldendrin', BIOCHEMISTRY-US, vol. 56, no. 19, pp. 2467-2476. https://doi.org/10.1021/acs.biochem.7b00132

APA

Kiran, U., Regur, P., Kreutz, M. R., Sharma, Y., & Chakraborty, A. (2017). Intermotif Communication Induces Hierarchical Ca(2+) Filling of Caldendrin. BIOCHEMISTRY-US, 56(19), 2467-2476. https://doi.org/10.1021/acs.biochem.7b00132

Vancouver

Kiran U, Regur P, Kreutz MR, Sharma Y, Chakraborty A. Intermotif Communication Induces Hierarchical Ca(2+) Filling of Caldendrin. BIOCHEMISTRY-US. 2017 May 16;56(19):2467-2476. https://doi.org/10.1021/acs.biochem.7b00132

Bibtex

@article{7be377ffa91643ed8f5cef4dd641f83b,
title = "Intermotif Communication Induces Hierarchical Ca(2+) Filling of Caldendrin",
abstract = "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.",
keywords = "Amino Acid Motifs, Amino Acid Substitution, Animals, Apoproteins, Binding Sites, Calcium Signaling, Calcium-Binding Proteins, Calorimetry, Circular Dichroism, Models, Molecular, Mutagenesis, Site-Directed, Mutation, Nerve Tissue Proteins, Protein Stability, Protein Unfolding, Rats, Recombinant Proteins, Spectrometry, Fluorescence, Thermodynamics, Titrimetry, Comparative Study, Journal Article",
author = "Uday Kiran and Phanindranath Regur and Kreutz, {Michael R} and Yogendra Sharma and Asima Chakraborty",
year = "2017",
month = may,
day = "16",
doi = "10.1021/acs.biochem.7b00132",
language = "English",
volume = "56",
pages = "2467--2476",
journal = "BIOCHEMISTRY-US",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "19",

}

RIS

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 -