1c1g

From Proteopedia

(Difference between revisions)

Revision as of 06:28, 11 August 2021

CRYSTAL STRUCTURE OF TROPOMYOSIN AT 7 ANGSTROMS RESOLUTION IN THE SPERMINE-INDUCED CRYSTAL FORM

Structural highlights

1c1g is a 4 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1c1g"

@@ Line 3: / Line 3: @@
 <StructureSection load='1c1g' size='340' side='right'caption='[[1c1g]], [[Resolution|resolution]] 7.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1c1g]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C1G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C1G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1c1g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C1G FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c1g OCA], [http://pdbe.org/1c1g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c1g RCSB], [http://www.ebi.ac.uk/pdbsum/1c1g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1c1g ProSAT]</span></td></tr>
+</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>
 </table>
 == Function ==
-[[http://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.
+[[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1c1g

From Proteopedia

Revision as of 06:28, 11 August 2021

CRYSTAL STRUCTURE OF TROPOMYOSIN AT 7 ANGSTROMS RESOLUTION IN THE SPERMINE-INDUCED CRYSTAL FORM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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