1aj3: Difference between revisions
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< | ==SOLUTION STRUCTURE OF THE SPECTRIN REPEAT, NMR, 20 STRUCTURES== | ||
<StructureSection load='1aj3' size='340' side='right'caption='[[1aj3]]' scene=''> | |||
You may | == 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 11:13, 22 May 2024
SOLUTION STRUCTURE OF THE SPECTRIN REPEAT, NMR, 20 STRUCTURESSOLUTION STRUCTURE OF THE SPECTRIN REPEAT, NMR, 20 STRUCTURES
Structural highlights
FunctionSPTN1_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCytoskeletal 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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