|
|
| Line 1: |
Line 1: |
| [[Image:1epu.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1epu.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1epu| PDB=1epu | SCENE= }} | | {{STRUCTURE_1epu| PDB=1epu | SCENE= }} |
|
| |
|
| '''X-RAY CRYSTAL STRUCTURE OF NEURONAL SEC1 FROM SQUID'''
| | ===X-RAY CRYSTAL STRUCTURE OF NEURONAL SEC1 FROM SQUID=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| BACKGROUND: Sec1-like molecules have been implicated in a variety of eukaryotic vesicle transport processes including neurotransmitter release by exocytosis. They regulate vesicle transport by binding to a t-SNARE from the syntaxin family. This process is thought to prevent SNARE complex formation, a protein complex required for membrane fusion. Whereas Sec1 molecules are essential for neurotransmitter release and other secretory events, their interaction with syntaxin molecules seems to represent a negative regulatory step in secretion. RESULTS: Here we report the X-ray crystal structure of a neuronal Sec1 homologue from squid, s-Sec1, at 2.4 A resolution. Neuronal s-Sec1 is a modular protein that folds into a V-shaped three-domain assembly. Peptide and mutagenesis studies are discussed with respect to the mechanism of Sec1 regulation. Comparison of the structure of squid s-Sec1 with the previously determined structure of rat neuronal Sec1 (n-Sec1) bound to syntaxin-1a indicates conformational rearrangements in domain III induced by syntaxin binding. CONCLUSIONS: The crystal structure of s-Sec1 provides the molecular scaffold for a number of molecular interactions that have been reported to affect Sec1 function. The structural differences observed between s-Sec1 and the structure of a rat n-Sec1-syntaxin-1a complex suggest that local conformational changes are sufficient to release syntaxin-1a from neuronal Sec1, an active process that is thought to involve additional effector molecule(s).
| | The line below this paragraph, {{ABSTRACT_PUBMED_10903948}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10903948 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_10903948}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| [[Category: Left-hand turn connection]] | | [[Category: Left-hand turn connection]] |
| [[Category: Parallel beta-sheet]] | | [[Category: Parallel beta-sheet]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:23:06 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:34:06 2008'' |
