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Crystallographic investigation and characterization of the interaction between presynaptic voltage-gated calcium channels and snare proteins Liu, Xiaohu
Abstract
Voltage-gated calcium channels (Cay) have functions ranging from regulating release of hormones and neurotransmitters, generating cardiac action potentials, and excitation-contraction coupling. At nerve terminals, N- and P/Q- type Cavs convert the action potential into aC²⁺ signal that in turn triggers neurotransmitter release. Neurotransmitter release requires several components, such as SNARE proteins. SNAREs, as well as many other presynaptic proteins, can interact with Cavs and inhibit them by increasing their inactivation. The interaction is localized in the intracellular loop between domains II and III of the CL 1 subunit, in a domain termed ‘synprint’ (synaptic protein interaction site). In this study, we tried to solve the structure of the synprint site by crystallography. To date, long needle-shape crystals were obtained; however, the quality of these crystals was not good enough for X-ray diffraction. in addition, isothermal titration calorimetry (ITC) was used to determine the interaction between SNARE protein syntaxinlA and the synprint site. It turned out that not any binding was detected, suggesting that the interaction between SNARE proteins and the presynaptic Cas, if at all present, is weak.
Item Metadata
Title |
Crystallographic investigation and characterization of the interaction between presynaptic voltage-gated calcium channels and snare proteins
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Creator | |
Publisher |
University of British Columbia
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Date Issued |
2010
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Description |
Voltage-gated calcium channels (Cay) have functions ranging from regulating
release of hormones and neurotransmitters, generating cardiac action potentials, and
excitation-contraction coupling. At nerve terminals, N- and P/Q- type Cavs convert the
action potential into aC²⁺ signal that in turn triggers neurotransmitter release.
Neurotransmitter release requires several components, such as SNARE proteins.
SNAREs, as well as many other presynaptic proteins, can interact with Cavs and inhibit
them by increasing their inactivation. The interaction is localized in the intracellular loop
between domains II and III of the CL 1 subunit, in a domain termed ‘synprint’ (synaptic
protein interaction site). In this study, we tried to solve the structure of the synprint site
by crystallography. To date, long needle-shape crystals were obtained; however, the
quality of these crystals was not good enough for X-ray diffraction. in addition,
isothermal titration calorimetry (ITC) was used to determine the interaction between
SNARE protein syntaxinlA and the synprint site. It turned out that not any binding was
detected, suggesting that the interaction between SNARE proteins and the presynaptic
Cas, if at all present, is weak.
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Genre | |
Type | |
Language |
eng
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Date Available |
2010-06-11
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Provider |
Vancouver : University of British Columbia Library
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Rights |
Attribution-NonCommercial-NoDerivatives 4.0 International
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DOI |
10.14288/1.0070992
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URI | |
Degree | |
Program | |
Affiliation | |
Degree Grantor |
University of British Columbia
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Graduation Date |
2010-05
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Campus | |
Scholarly Level |
Graduate
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Rights URI | |
Aggregated Source Repository |
DSpace
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Rights
Attribution-NonCommercial-NoDerivatives 4.0 International