This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1ic2

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

DECIPHERING THE DESIGN OF THE TROPOMYOSIN MOLECULE

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ic2"

@@ Line 1: / Line 1: @@
-[[Image:1ic2.gif|left|200px]]<br /><applet load="1ic2" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1ic2, resolution 2.0&Aring;" />
-'''DECIPHERING THE DESIGN OF THE TROPOMYOSIN MOLECULE'''<br />
-==Overview==
+==DECIPHERING THE DESIGN OF THE TROPOMYOSIN MOLECULE==
-The crystal structure at 2.0-A resolution of an 81-residue N-terminal, fragment of muscle alpha-tropomyosin reveals a parallel two-stranded, alpha-helical coiled-coil structure with a remarkable core. The high, alanine content of the molecule is clustered into short regions where the, local 2-fold symmetry is broken by a small (approximately 1.2-A) axial, staggering of the helices. The joining of these regions with neighboring, segments, where the helices are in axial register, gives rise to specific, bends in the molecular axis. We observe such bends to be widely, distributed in two-stranded alpha-helical coiled-coil proteins. This, asymmetric design in a dimer of identical (or highly similar) sequences, allows the tropomyosin molecule to adopt multiple bent conformations. The, seven alanine clusters in the core of the complete molecule (which spans, seven monomers of the actin helix) promote the semiflexible winding of the, tropomyosin filament necessary for its regulatory role in muscle, contraction.
+<StructureSection load='1ic2' size='340' side='right'caption='[[1ic2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ic2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IC2 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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=1ic2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ic2 OCA], [https://pdbe.org/1ic2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ic2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ic2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ic2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TPM1_CHICK TPM1_CHICK] 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/ic/1ic2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ic2 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-IC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IC2 OCA].
+*[[Tropomyosin 3D structures|Tropomyosin 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Deciphering the design of the tropomyosin molecule., Brown JH, Kim KH, Jun G, Greenfield NJ, Dominguez R, Volkmann N, Hitchcock-DeGregori SE, Cohen C, Proc Natl Acad Sci U S A. 2001 Jul 17;98(15):8496-501. Epub 2001 Jul 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11438684 11438684]
 [[Category: Gallus gallus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Brown, J.H.]]
+[[Category: Brown JH]]
-[[Category: Cohen, C.]]
+[[Category: Cohen C]]
-[[Category: Dominguez, R.]]
+[[Category: Dominguez R]]
-[[Category: Greenfield, N.J.]]
+[[Category: Greenfield NJ]]
-[[Category: Hitchcock-DeGregori, S.E.]]
+[[Category: Hitchcock-DeGregori SE]]
-[[Category: Jun, G.]]
+[[Category: Jun G]]
-[[Category: Kim, K.H.]]
+[[Category: Kim K-H]]
-[[Category: Volkmann, N.]]
+[[Category: Volkmann N]]
-[[Category: alanine]]
-[[Category: alpha-helical coiled coil]]
-[[Category: axial stagger]]
-[[Category: bend]]
-[[Category: symmetry]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:16:30 2007''

1ic2

From Proteopedia

Current revision

DECIPHERING THE DESIGN OF THE TROPOMYOSIN MOLECULE

Structural highlights

Function

Evolutionary Conservation

See Also

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox