1aj3: Difference between revisions
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New page: left|200px<br /><applet load="1aj3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aj3" /> '''SOLUTION STRUCTURE OF THE SPECTRIN REPEAT, N... |
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== | ==SOLUTION STRUCTURE OF THE SPECTRIN REPEAT, NMR, 20 STRUCTURES== | ||
Cytoskeletal proteins belonging to the spectrin family have an elongated | <StructureSection load='1aj3' size='340' side='right'caption='[[1aj3]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1aj3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AJ3 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1aj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aj3 OCA], [https://pdbe.org/1aj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aj3 RCSB], [https://www.ebi.ac.uk/pdbsum/1aj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aj3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SPTN1_CHICK SPTN1_CHICK] Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization. | |||
== 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/aj/1aj3_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=1aj3 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cytoskeletal proteins belonging to the spectrin family have an elongated structure composed of repetitive units. The three-dimensional solution structure of the 16th repeat from chicken brain alpha-spectrin (R16) has been determined by NMR spectroscopy and distance geometry-simulated annealing calculations. We used a total of 1035 distance restraints, which included 719 NOE-based values obtained by applying the ambiguous restraints for iterative assignment (ARIA) method. In addition, we performed a direct refinement against 1H-chemical shifts. The final ensemble of 20 structures shows an average RMSD of 1.52 A from the mean for the backbone atoms, excluding loops and N and C termini. R16 is made up of three antiparallel alpha-helices separated by two loops, and folds into a left-handed coiled-coil. The basic unit of spectrin is an antiparallel heterodimer composed of two homologous chains, beta and alpha. These assemble a tetramer via a mechanism that relies on the completion of a single repeat by association of the partial repeats located at the C terminus of the beta-chain (two helices) and at the N terminus of the alpha-chain (one helix). This tetramer is the assemblage able to cross-link actin filaments. Model building by homology of the "tetramerization" repeat from human erythrocyte spectrin illuminates the possible role of point mutations which cause hemolytic anemias. | |||
Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil.,Pascual J, Pfuhl M, Walther D, Saraste M, Nilges M J Mol Biol. 1997 Oct 31;273(3):740-51. PMID:9356261<ref>PMID:9356261</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1aj3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Spectrin 3D structures|Spectrin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Nilges | [[Category: Nilges M]] | ||
[[Category: Pascual | [[Category: Pascual J]] | ||
[[Category: Pfuhl | [[Category: Pfuhl M]] | ||
[[Category: Saraste | [[Category: Saraste M]] | ||
[[Category: Walther | [[Category: Walther D]] | ||
Latest revision as of 08:13, 22 May 2024
SOLUTION STRUCTURE OF THE SPECTRIN REPEAT, NMR, 20 STRUCTURES
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