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| {{STRUCTURE_2r83| PDB=2r83 | SCENE= }} | | {{STRUCTURE_2r83| PDB=2r83 | SCENE= }} |
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| '''Crystal structure analysis of human synaptotagmin 1 C2A-C2B'''
| | ===Crystal structure analysis of human synaptotagmin 1 C2A-C2B=== |
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| ==Overview==
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| Release of neurotransmitter from synaptic vesicles requires the Ca2+/phospholipid-binding protein synaptotagmin 1. There is considerable evidence that cooperation between the tandem C2 domains of synaptotagmin is a requirement of regulated exocytosis; however, high-resolution structural evidence for this interaction has been lacking. The 2.7 A crystal structure of the cytosolic domains of human synaptotagmin 1 in the absence of Ca2+ reveals a novel closed conformation of the protein. The shared interface between C2A and C2B is stabilized by a network of interactions between residues on the C-terminal alpha-helix of the C2B domain and residues on loops 1-3 of the Ca2+-binding region of C2A. These interactions alter the overall shape of the Ca2+-binding pocket of C2A, but not that of C2B. Thus, synaptotagmin 1 C2A-C2B may utilize a novel regulatory mechanism whereby one C2 domain could regulate the other until an appropriate triggering event decouples them.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17956130}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17956130 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17956130}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Synapse]] | | [[Category: Synapse]] |
| [[Category: Transmembrane]] | | [[Category: Transmembrane]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:24:30 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:30:26 2008'' |