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InterPro: IPR000533 Tropomyosin
Protein matches
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UniProtKB Matches: 632 proteins |
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Accession
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IPR000533 Tropomyosin |
Type
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Signatures
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Tropomyosins [1], are a family of closely related proteins present in muscle and non-muscle cells. In striated muscle, tropomyosin mediate the interactions between the troponin complex and actin so as to regulate muscle contraction [2]. The role of tropomyosin in smooth muscle and non-muscle tissues is not clear. Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites [3]. There are multiple cell-specific isoforms, created by differential splicing of the messenger RNA from one gene, but the proportions of the isoforms vary between different cell types. Muscle isoforms of tropomyosin are characterised by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Some of the proteins in this family are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee
King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E.,
Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of
the first three letters of the genus; a space; the first letter of the
species name; a space and an arabic number. In the event that two species
names have identical designations, they are discriminated from one another
by adding one or more letters (as necessary) to each species designation.
The allergens in this family include allergens with the following designations: Met e 1.
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Structural links
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Database links
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Additional Reading
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Greenfield NJ, Huang YJ, Palm T, Swapna GV, Monleon D, Montelione GT, Hitchcock-DeGregori SE.
Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein.
J. Mol. Biol. 312 2001 833-47
[PubMed: 11575936]
http://dx.doi.org/10.1006/jmbi.2001.4982
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Greenfield NJ, Swapna GV, Huang Y, Palm T, Graboski S, Montelione GT, Hitchcock-DeGregori SE.
The structure of the carboxyl terminus of striated alpha-tropomyosin in solution reveals an unusual parallel arrangement of interacting alpha-helices.
Biochemistry 42 2003 614-9
[PubMed: 12534273]
http://dx.doi.org/10.1021/bi026989e
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Greenfield NJ, Huang YJ, Swapna GV, Bhattacharya A, Rapp B, Singh A, Montelione GT, Hitchcock-DeGregori SE.
Solution NMR structure of the junction between tropomyosin molecules: implications for actin binding and regulation.
J. Mol. Biol. 364 2006 80-96
[PubMed: 16999976]
http://dx.doi.org/10.1016/j.jmb.2006.08.033
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Whitby FG, Phillips GN Jr.
Crystal structure of tropomyosin at 7 Angstroms resolution.
Proteins 38 2000 49-59
[PubMed: 10651038]
http://dx.doi.org/10.1002/(SICI)1097-0134(20000101)38:1<49::AID-PROT6>3.3.CO;2-2
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Brown JH, Zhou Z, Reshetnikova L, Robinson H, Yammani RD, Tobacman LS, Cohen C.
Structure of the mid-region of tropomyosin: bending and binding sites for actin.
Proc. Natl. Acad. Sci. U.S.A. 102 2005 18878-83
[PubMed: 16365313]
http://dx.doi.org/10.1073/pnas.0509269102
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InterPro 24.0
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