1MV4

TM9A251-284: A Peptide Model of the C-Terminus of a Rat Striated Alpha Tropomyosin

Summary for 1MV4

• Entry DOI: 10.2210/pdb1mv4/pdb
• Related: 1IC2 1IHQ 1TMZ
• NMR Information: BMRB: 5610
• Descriptor: Tropomyosin 1 alpha chain (1 entity in total)
• Functional Keywords: tropomyosin, exon 9a, actin-binding, troponin binding, muscle, alpha-helix, coiled-coil, dimer, peptide-model, two-chained, disulfide cross-linked, de novo protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm, cytoskeleton: P04692
• Total number of polymer chains: 2
• Total formula weight: 8355.41

Authors

Greenfield, N.J.,Swapna, G.V.T.,Huang, Y.,Palm, T.,Graboski, S.,Montelione, G.T.,Hitchcock-Degregori, S.E. (deposition date: 2002-09-24, release date: 2003-02-18, Last modification date: 2022-02-23)

• Primary citation: Greenfield, N.J.,Swapna, G.V.T.,Huang, Y.,Palm, T.,Graboski, S.,Montelione, G.T.,Hitchcock-DeGregori, S.E.; The Structure of the Carboxyl Terminus of Striated alpha-Tropomyosin in Solution Reveals an Unusual Parallel Arrangement of Interacting alpha-Helices; Biochemistry, 42:614-619, 2003; PubMed: 12534273; DOI: 10.1021/bi026989e

Experimental method

SOLUTION NMR