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1u4q

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[[Image:1u4q.gif|left|200px]]
 
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==Crystal Structure of Repeats 15, 16 and 17 of Chicken Brain Alpha Spectrin==
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The line below this paragraph, containing "STRUCTURE_1u4q", creates the "Structure Box" on the page.
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<StructureSection load='1u4q' size='340' side='right'caption='[[1u4q]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1u4q]] is a 2 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=1U4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U4Q FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u4q OCA], [https://pdbe.org/1u4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u4q RCSB], [https://www.ebi.ac.uk/pdbsum/1u4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u4q ProSAT]</span></td></tr>
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{{STRUCTURE_1u4q| PDB=1u4q | SCENE= }}
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u4/1u4q_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1u4q ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of Repeats 15, 16 and 17 of Chicken Brain Alpha Spectrin'''
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==See Also==
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*[[Spectrin 3D structures|Spectrin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Previous X-ray crystal structures have shown that linkers of five amino acid residues connecting pairs of chicken brain alpha-spectrin and human erythroid beta-spectrin repeats can undergo bending without losing their alpha-helical structure. To test whether bending at one linker can influence bending at an adjacent linker, the structures of two and three repeat fragments of chicken brain alpha-spectrin have been determined by X-ray crystallography. The structure of the three-repeat fragment clearly shows that bending at one linker can occur independently of bending at an adjacent linker. This observation increases the possible trajectories of modeled chains of spectrin repeats. Furthermore, the three-repeat molecule crystallized as an antiparallel dimer with a significantly smaller buried interfacial area than that of alpha-actinin, a spectrin-related molecule, but large enough and of a type indicating biological specificity. Comparison of the structures of the spectrin and alpha-actinin dimers supports weak association of the former, which could not be detected by analytical ultracentrifugation, versus strong association of the latter, which has been observed by others. To correlate features of the structure with solution properties and to test a previous model of stable spectrin and dystrophin repeats, the number of inter-helical interactions in each repeat of several spectrin structures were counted and compared to their thermal stabilities. Inter-helical interactions, but not all interactions, increased in parallel with measured thermal stabilities of each repeat and in agreement with the thermal stabilities of two and three repeats and also partial repeats of spectrin.
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==About this Structure==
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1U4Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U4Q OCA].
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==Reference==
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Independent movement, dimerization and stability of tandem repeats of chicken brain alpha-spectrin., Kusunoki H, Minasov G, Macdonald RI, Mondragon A, J Mol Biol. 2004 Nov 19;344(2):495-511. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15522301 15522301]
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kusunoki, H.]]
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[[Category: Kusunoki H]]
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[[Category: MacDonald, R I.]]
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[[Category: MacDonald RI]]
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[[Category: Minasov, G.]]
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[[Category: Minasov G]]
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[[Category: Mondragon, A.]]
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[[Category: Mondragon A]]
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[[Category: 3-helix coiled-coil]]
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[[Category: Alpha spectrin]]
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[[Category: Alpha-helical linker region]]
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[[Category: Three repeats of spectrin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:45:41 2008''
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Current revision

Crystal Structure of Repeats 15, 16 and 17 of Chicken Brain Alpha Spectrin

PDB ID 1u4q

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