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PMID:9096343
| Citation |
Weimbs, T, Low, SH, Chapin, SJ, Mostov, KE, Bucher, P and Hofmann, K (1997) A conserved domain is present in different families of vesicular fusion proteins: a new superfamily. Proc. Natl. Acad. Sci. U.S.A. 94:3046-51 |
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| Abstract |
We have analyzed conserved domains in t-SNAREs [soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors in the target membrane], proteins that are believed to be involved in the fusion of transport vesicles with their target membrane. By using a sensitive computer method, the generalized profile method, we were able to identify a new homology domain that is common in the two protein families previously identified to act as t-SNAREs, the syntaxin and SNAP-25 (synaptosome-associated protein of 25 kDa) families, which therefore constitute a new superfamily. This homology domain of approximately 60 amino acids is predicted to form a coiled-coil structure. The significance of this homology domain could be demonstrated by a partial suppression of the coiled-coil properties of the domain profile. In proteins belonging to the syntaxin family, a single homology domain is located near the transmembrane domain, whereas the members of the SNAP-25 family possess two homology domains. This domain was also identified in several proteins that have been implicated in vesicular transport but do not belong to any of the t-SNARE protein families. Several new yeast, nematode, and mammalian proteins were identified that belong to the new superfamily. The evolutionary conservation of the SNARE coiled-coil homology domain suggests that this domain has a similar function in different membrane fusion proteins. |
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| Keywords |
Amino Acid Sequence; Conserved Sequence; Membrane Fusion; Membrane Proteins/chemistry; Molecular Sequence Data; Nerve Tissue Proteins/chemistry; Nerve Tissue Proteins/physiology; Protein Conformation; Qa-SNARE Proteins; Sequence Homology, Amino Acid; Synaptosomal-Associated Protein 25 |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
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See also
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