Tropomyosin: Difference between revisions
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<references/><references/>{{ | <references/><references/>{{STRUCTURE_2b9c|PDB=2b9c |SCENE= caption='Rat tropomyosin mid region [[2b9c]]'}} | ||
[[Image:Tropomyosin Dimer-2.png | thumb | left| 300x180px | alt text | '''Tropomyosin:''' Coiled-Coil Dimer, which is composed of two alpha helices [http://www.pdb.org/pdb/explore/explore.do?structureId=1C1G (1C1G)] ]][[Image:B Lehman1.jpg | thumb | 300 x 430px | left | alt text | '''Tropomyosin''' (seen in yello and red) wrapped around actin filaments, which are EM reconstructions with G-actin ribbion structures filling in the EM structure. (Picture generated from William Lehman's [http://www.bumc.bu.edu/phys-biophys/research/filhel/ Website]) ]]'''[[Tropomyosin]] (TM)''' is an [[actin]] binding protein, which consists of a coiled-coil dimer (see left) and forms a polymer along the length of actin by a head-to-tail overlap along the major grove of actin (see down & left)<ref name="Gunning">Tropomyosins. I. Gunning, Peter, 1950- II. Series.[DNLM: 1. Tropomyosin. W1 AD559 v.644 2008 / WE 500 T856 2008]</ref>. The head-to-tail overlap allows flexibility between the tropomyosin dimers so it will lay unstrained along the filament<ref name="Gunning"/>. Each tropomyosin molecule spans seven actin monomers within a filament and lays N- to C- terminally from actin's pointed to barbed end<ref name="Frye">PMID:20465283</ref>. The 284 amino acid helix has a length of 420 Angstroms and has a molecular weight around 65-70 kilodaltons (vertebrate tropomyosin)<ref name="Gunning"/><ref name="Whitby">PMID:10651038</ref>. A few of tropomyosin's characteristics as an actin binding protein includes regulation, stabilization and recruitment. | [[Image:Tropomyosin Dimer-2.png | thumb | left| 300x180px | alt text | '''Tropomyosin:''' Coiled-Coil Dimer, which is composed of two alpha helices [http://www.pdb.org/pdb/explore/explore.do?structureId=1C1G (1C1G)] ]][[Image:B Lehman1.jpg | thumb | 300 x 430px | left | alt text | '''Tropomyosin''' (seen in yello and red) wrapped around actin filaments, which are EM reconstructions with G-actin ribbion structures filling in the EM structure. (Picture generated from William Lehman's [http://www.bumc.bu.edu/phys-biophys/research/filhel/ Website]) ]]'''[[Tropomyosin]] (TM)''' is an [[actin]] binding protein, which consists of a coiled-coil dimer (see left) and forms a polymer along the length of actin by a head-to-tail overlap along the major grove of actin (see down & left)<ref name="Gunning">Tropomyosins. I. Gunning, Peter, 1950- II. Series.[DNLM: 1. Tropomyosin. W1 AD559 v.644 2008 / WE 500 T856 2008]</ref>. The head-to-tail overlap allows flexibility between the tropomyosin dimers so it will lay unstrained along the filament<ref name="Gunning"/>. Each tropomyosin molecule spans seven actin monomers within a filament and lays N- to C- terminally from actin's pointed to barbed end<ref name="Frye">PMID:20465283</ref>. The 284 amino acid helix has a length of 420 Angstroms and has a molecular weight around 65-70 kilodaltons (vertebrate tropomyosin)<ref name="Gunning"/><ref name="Whitby">PMID:10651038</ref>. A few of tropomyosin's characteristics as an actin binding protein includes regulation, stabilization and recruitment. | ||