1tud: Difference between revisions

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New page: left|200px<br /><applet load="1tud" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tud, resolution 1.77Å" /> '''ALPHA-SPECTRIN SRC H...
 
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[[Image:1tud.jpg|left|200px]]<br /><applet load="1tud" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1tud, resolution 1.77&Aring;" />
'''ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT N47-D48'''<br />


==Overview==
==ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT N47-D48==
We have analyzed the structure, stability and folding kinetics of, circularly permuted forms of alpha-spectrin SH3 domain. All the possible, permutations involving the disruption of the covalent linkage between two, beta-strands forming a beta-hairpin have been done. The different proteins, constructed here fold to a native conformation similar to that of, wild-type protein, as demonstrated by nuclear magnetic resonance and, circular dichroism. Although all the mutants have similar stabilities, (they are 1 to 2 kcal mol-1 less stable than the wild-type) their rate, constants for folding and unfolding are quite different. Protein, engineering, in combination with kinetics indicates that the folding, pathway has been changed in the circularly permuted proteins. We conclude, that neither the order of secondary structure elements, nor the, preservation of any of the beta-hairpins present in this domain, is, crucial for the ability of the polypeptide to fold, but they influence the, folding and unfolding kinetics and could determine its folding pathway.
<StructureSection load='1tud' size='340' side='right'caption='[[1tud]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1tud]] is a 1 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=1TUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TUD 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]] 1.77&#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=1tud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tud OCA], [https://pdbe.org/1tud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tud RCSB], [https://www.ebi.ac.uk/pdbsum/1tud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tud 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/tu/1tud_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=1tud ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1TUD 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=1TUD OCA].
*[[Spectrin 3D structures|Spectrin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics., Viguera AR, Blanco FJ, Serrano L, J Mol Biol. 1995 Apr 7;247(4):670-81. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7723022 7723022]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Serrano, L.]]
[[Category: Serrano L]]
[[Category: Viguera, A.R.]]
[[Category: Viguera AR]]
[[Category: Wilmanns, M.]]
[[Category: Wilmanns M]]
[[Category: calcium-binding]]
[[Category: capping protein]]
[[Category: cytoskeleton]]
[[Category: duplication]]
[[Category: repeat]]
[[Category: sh3 domain]]
 
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Latest revision as of 08:42, 14 February 2024

ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT N47-D48

1tud, resolution 1.77Å

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