File:Muncprotein.jpg: Difference between revisions
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The crystal structures of a Munc13-1 homodimer (top) and a Munc13-1/RIM2α heterodimer (bottom) show how a C2 domain participates in two distinct protein–protein interactions that might couple synaptic vesicle priming to presynaptic plasticity. | The crystal structures of a Munc13-1 homodimer (top) and a Munc13-1/RIM2α heterodimer (bottom) show how a C2 domain participates in two distinct protein–protein interactions that might couple synaptic vesicle priming to presynaptic plasticity. | ||
From: Shape of a Common Protein Module Suggests Role as Molecular Switch Inman M PLoS Biology Vol. 4, No. 7, e221 doi:10.1371/journal.pbio.0040221 | From: [http://biology.plosjournals.org/perlserv/?request=get-document&doi=10.1371/journal.pbio.0040221 Shape of a Common Protein Module Suggests Role as Molecular Switch Inman M PLoS Biology Vol. 4, No. 7, e221 doi:10.1371/journal.pbio.0040221] | ||
Image: http://biology.plosjournals.org/perlserv/?request=slideshow&type=figure&doi=10.1371/journal.pbio.0040221&id=57720 | Image: http://biology.plosjournals.org/perlserv/?request=slideshow&type=figure&doi=10.1371/journal.pbio.0040221&id=57720 | ||
{{cc-by-2.5}} | {{cc-by-2.5}} | ||
Revision as of 20:35, 22 June 2007
The crystal structures of a Munc13-1 homodimer (top) and a Munc13-1/RIM2α heterodimer (bottom) show how a C2 domain participates in two distinct protein–protein interactions that might couple synaptic vesicle priming to presynaptic plasticity.
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