Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC50192t-SNARE coiled-coil homology domain profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC50192
The process of vesicular membrane fusion in eukaryotic cells depends on a conserved fusion machinery called SNARE (soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors). In the process of vesicle docking, proteins present on the vesicle (v-SNARE) have to bind to their counterpart on the target membrane (t-SNARE) to form a core complex that can then recruit the soluble proteins NSF and SNAP. This so called fusion complex can then disassemble after ATP hydrolysis mediated by the ATPase NSF in a process that leads to membrane fusion and the release of the vesicle contents. t-SNAREs consist of two different families of proteins: the type II integral membrane proteins syntaxins and SNAP-25 (synaptosome-associated protein of 25 kDa), which is anchored in the plasma membrane by attached lipids and does not span the membrane [1].
The N- and C-terminal coiled-coil domains of members of the SNAP-25 family and the most C-terminal coiled-coil domain of the syntaxin family are related to each other and form a new homology domain of approximately 60 amino acids. This domain is also found in other known proteins involved in vesicular membrane traffic, some of which belong to different protein families [1]:
- Yeast SFT1, UFE1, BET1, VAM7 and YDR468c proteins.
- Mammalian TSL-4 proteins.
The profile we developed covers the entire t-SNARE coiled-coil homology domain.
Last update:April 2002 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Weimbs T. Low S.H. Chapin S.J. Mostov K.E. Bucher P. Hofmann K. |
| Title | A conserved domain is present in different families of vesicular fusion proteins: a new superfamily. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 94:3046-3051(1997). | |
| PubMed ID | 9096343 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.