2kr3: Difference between revisions
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==Solution structure of SHA-D== | |||
<StructureSection load='2kr3' size='340' side='right'caption='[[2kr3]]' scene=''> | |||
== Structural highlights == | |||
<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='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> | |||
</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/kr/2kr3_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=2kr3 ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[Spectrin 3D structures|Spectrin 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | |||
[[Category: Large Structures]] | |||
[[Category: Filimonov VV]] | |||
[[Category: Gushchina LV]] | |||
[[Category: Khristoforov VS]] | |||
[[Category: Kudrevatykh YA]] | |||
[[Category: Kutyshenko VP]] | |||
[[Category: Prokhorov DA]] | |||
[[Category: Timchenko MA]] | |||
Latest revision as of 09:47, 1 May 2024
Solution structure of SHA-DSolution structure of SHA-D
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. See Also |
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