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2kr3
From Proteopedia
(Difference between revisions)
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==Solution structure of SHA-D== | ==Solution structure of SHA-D== | ||
| - | <StructureSection load='2kr3' size='340' side='right'caption='[[2kr3 | + | <StructureSection load='2kr3' size='340' side='right'caption='[[2kr3]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2kr3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2kr3]] 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=2KR3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KR3 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2kr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kr3 OCA], [https://pdbe.org/2kr3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kr3 RCSB], [https://www.ebi.ac.uk/pdbsum/2kr3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kr3 ProSAT]</span></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=2kr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kr3 OCA], [https://pdbe.org/2kr3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kr3 RCSB], [https://www.ebi.ac.uk/pdbsum/2kr3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kr3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=2kr3 ConSurf]. | </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=2kr3 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Protein SHA-D of "SH3-Bergerac" chimeric proteins family was constructed by substitution of beta-turn N47-D48 in spectrin SH3-domain by KATANDKTYE amino acid sequence. Structural and dynamics properties of SHA-D in solution were studied by with the help of high-resolution NMR. The extension of SHA-D polypeptide chain in comparison with wild type of protein WT-SH3 (~ 17%) practically doesn't affect almost the total molecule topology. 3D-structure of SHA-D is practically identical to the proteins of "SH3-Bergerac" family. However there are some differences in dynamic characteristics in the region of substitution. The G52D substitution in SHA-D protein results in a destabilization of the region insertion where the conditions for conformational exchange appear. Destabilization further affects the entire SHA- D molecule making its structure more labile. | ||
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| - | [Chimeric SHA-D domain ("SH3-Bergerac"): 3D-structure and dynamics studies in solution],Khristophorov VS, Prokhorov DA, Timchenko MA, Kudrevatykh IuA, Gushchina LV, Filimonov VV, Kutyshenko VP Bioorg Khim. 2010 Jul-Aug;36(4):505-13. PMID:20823919<ref>PMID:20823919</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2kr3" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Spectrin|Spectrin]] | + | *[[Spectrin 3D structures|Spectrin 3D structures]] |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Gallus gallus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Filimonov | + | [[Category: Filimonov VV]] |
| - | [[Category: Gushchina | + | [[Category: Gushchina LV]] |
| - | [[Category: Khristoforov | + | [[Category: Khristoforov VS]] |
| - | [[Category: Kudrevatykh | + | [[Category: Kudrevatykh YA]] |
| - | [[Category: Kutyshenko | + | [[Category: Kutyshenko VP]] |
| - | [[Category: Prokhorov | + | [[Category: Prokhorov DA]] |
| - | [[Category: Timchenko | + | [[Category: Timchenko MA]] |
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Current revision
Solution structure of SHA-D
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