000114860 001__ 114860
000114860 005__ 20190527151553.0
000114860 0247_ $$2doi$$a10.1073/pnas.94.7.3046
000114860 037__ $$aARTICLE
000114860 245__ $$aA conserved domain is present in different families of vesicular fusion proteins: a new superfamily
000114860 269__ $$a1997
000114860 260__ $$c1997
000114860 336__ $$aJournal Articles
000114860 500__ $$aDepartment of Anatomy, University of California, San Francisco 94143-0452, USA. weimbs@itsa.ucsf.edu
000114860 520__ $$aWe have analyzed conserved domains in t-SNAREs [soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors in the target membrane], proteins that are believed to be involved in the fusion of transport vesicles with their target membrane. By using a sensitive computer method, the generalized profile method, we were able to identify a new homology domain that is common in the two protein families previously identified to act as t-SNAREs, the syntaxin and SNAP-25 (synaptosome-associated protein of 25 kDa) families, which therefore constitute a new superfamily. This homology domain of approximately 60 amino acids is predicted to form a coiled-coil structure. The significance of this homology domain could be demonstrated by a partial suppression of the coiled-coil properties of the domain profile. In proteins belonging to the syntaxin family, a single homology domain is located near the transmembrane domain, whereas the members of the SNAP-25 family possess two homology domains. This domain was also identified in several proteins that have been implicated in vesicular transport but do not belong to any of the t-SNARE protein families. Several new yeast, nematode, and mammalian proteins were identified that belong to the new superfamily. The evolutionary conservation of the SNARE coiled-coil homology domain suggests that this domain has a similar function in different membrane fusion proteins.
000114860 700__ $$aWeimbs, T.
000114860 700__ $$aLow, S. H.
000114860 700__ $$aChapin, S. J.
000114860 700__ $$aMostov, K. E.
000114860 700__ $$0244404$$g113607$$aBucher, P.
000114860 700__ $$aHofmann, K.
000114860 773__ $$j94$$tProceedings Of The National Academy Of Sciences Of The United States Of America$$k7$$q3046-51
000114860 909C0 $$xU11780$$0252244$$pGR-BUCHER
000114860 909CO $$pSV$$particle$$ooai:infoscience.tind.io:114860
000114860 937__ $$aGR-BUCHER-ARTICLE-1997-005
000114860 973__ $$rREVIEWED$$sPUBLISHED$$aOTHER
000114860 980__ $$aARTICLE