1c1g

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c1g OCA], [https://pdbe.org/1c1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c1g RCSB], [https://www.ebi.ac.uk/pdbsum/1c1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c1g ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/TPM1_PIG TPM1_PIG]] Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.

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== Publication Abstract from PubMed ==

Tropomyosin is a 400A-long coiled coil that polymerizes to form a continuous filament that associates with actin in muscle and numerous non-muscle cells. Tropomyosin and troponin together form a calcium-sensitive switch that is responsible for thin-filament regulation of striated muscle. Subtle structural features of the molecule, including non-canonical aspects of its coiled-coil motif, undoubtedly influence its association with f-actin and its role in thin filament regulation. Previously, careful inspection of native diffraction intensities was sufficient to construct a model of tropomyosin at 9A resolution in a spermine-induced crystal form that diffracts anisotropically to 4A resolution. Single isomorphous replacement (SIR) phasing has now provided an empirical determination of the structure at 7A resolution. A novel method of heavy-atom analysis was used to overcome difficulties in interpretation of extremely anisotropic diffraction. The packing arrangement of the molecules in the crystal, and important aspects of the tropomyosin geometry such as non-uniformities of the pitch and variable bending and radius of the coiled coil are evident.

Crystal structure of tropomyosin at 7 Angstroms resolution.,Whitby FG, Phillips GN Jr Proteins. 2000 Jan 1;38(1):49-59. PMID:10651038<ref>PMID:10651038</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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[[Category: Phillips, G N]]

[[Category: Whitby, F G]]

[[Category: Tropomyosin coiled-coil alpha-helical]]