This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2kr3
From Proteopedia
(Difference between revisions)
| (4 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| + | |||
==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 [ | + | <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><td class="sblockLbl"><b>[[ | + | </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=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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </table> |
| - | <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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kr/2kr3_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kr/2kr3_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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. | ||
| - | |||
| - | [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> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
==See Also== | ==See Also== | ||
| - | *[[Spectrin|Spectrin]] | + | *[[Spectrin 3D structures|Spectrin 3D structures]] |
| - | + | ||
| - | + | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
| - | [[Category: Filimonov | + | [[Category: Large Structures]] |
| - | [[Category: Gushchina | + | [[Category: Filimonov VV]] |
| - | [[Category: Khristoforov | + | [[Category: Gushchina LV]] |
| - | [[Category: Kudrevatykh | + | [[Category: Khristoforov VS]] |
| - | [[Category: Kutyshenko | + | [[Category: Kudrevatykh YA]] |
| - | [[Category: Prokhorov | + | [[Category: Kutyshenko VP]] |
| - | [[Category: Timchenko | + | [[Category: Prokhorov DA]] |
| - | + | [[Category: Timchenko MA]] | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Solution structure of SHA-D
| |||||||||||
