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2b9c

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Structure of tropomyosin's mid-region: bending and binding sites for actin

Structural highlights

2b9c is a 2 chain structure with sequence from Rattus norvegicus. 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_RAT 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 two-chain alpha-helical coiled coil whose periodic interactions with the F-actin helix are critical for thin filament stabilization and the regulation of muscle contraction. Here we deduce the mechanical and chemical basis of these interactions from the 2.3-A-resolution crystal structure of the middle three of tropomyosin's seven periods. Geometrically specific bends of the coiled coil, produced by clusters of core alanines, and variable bends about gaps in the core, produced by isolated alanines, occur along the molecule. The crystal packing is notable in signifying that the functionally important fifth period includes an especially favorable protein-binding site, comprising an unusual apolar patch on the surface together with surrounding charged residues. Based on these and other results, we have constructed a specific model of the thin filament, with the N-terminal halves of each period (i.e., the so-called "alpha zones") of tropomyosin axially aligned with subdomain 3 of each monomer in F-actin.

Structure of the mid-region of tropomyosin: bending and binding sites for actin.,Brown JH, Zhou Z, Reshetnikova L, Robinson H, Yammani RD, Tobacman LS, Cohen C Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18878-83. Epub 2005 Dec 19. PMID:16365313^[1]

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

References

↑ 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. 2005 Dec 27;102(52):18878-83. Epub 2005 Dec 19. PMID:16365313

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/2b9c"

@@ Line 1: / Line 1: @@
 ==Structure of tropomyosin's mid-region: bending and binding sites for actin==
-<StructureSection load='2b9c' size='340' side='right' caption='[[2b9c]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='2b9c' size='340' side='right'caption='[[2b9c]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2b9c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B9C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B9C FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2b9c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B9C 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=2b9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b9c OCA], [http://pdbe.org/2b9c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b9c RCSB], [http://www.ebi.ac.uk/pdbsum/2b9c PDBsum]</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=2b9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b9c OCA], [https://pdbe.org/2b9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b9c RCSB], [https://www.ebi.ac.uk/pdbsum/2b9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b9c ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TPM1_RAT TPM1_RAT]] 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_RAT TPM1_RAT] 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]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b9/2b9c_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b9/2b9c_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 33: / Line 34: @@
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
+[[Category: Large Structures]]
-[[Category: Brown, J H]]
+[[Category: Rattus norvegicus]]
-[[Category: Cohen, C]]
+[[Category: Brown JH]]
-[[Category: Reshetnikova, L]]
+[[Category: Cohen C]]
-[[Category: Robinson, H]]
+[[Category: Reshetnikova L]]
-[[Category: Tobacman, L S]]
+[[Category: Robinson H]]
-[[Category: Yammani, R D]]
+[[Category: Tobacman LS]]
-[[Category: Zhou, Z]]
+[[Category: Yammani RD]]
-[[Category: Alanine]]
+[[Category: Zhou Z]]
-[[Category: Alpha-helix]]
-[[Category: Axial stagger]]
-[[Category: Cardiomyopathy]]
-[[Category: Contractile protein]]
-[[Category: Crystal packing]]
-[[Category: Elongated protein]]
-[[Category: Radius]]
-[[Category: Side-chain packing]]
-[[Category: Temperature factor]]

2b9c

From Proteopedia

Current revision

Structure of tropomyosin's mid-region: bending and binding sites for actin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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