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==CRYSTAL STRUCTURE OF A SRC-HOMOLOGY 3 (SH3) DOMAIN== | |||
<StructureSection load='1shg' size='340' side='right'caption='[[1shg]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1shg]] 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=1SHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SHG 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]] 1.8Å</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=1shg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1shg OCA], [https://pdbe.org/1shg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1shg RCSB], [https://www.ebi.ac.uk/pdbsum/1shg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1shg ProSAT]</span></td></tr> | |||
== | </table> | ||
[[1shg]] is a 1 chain structure | == 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/sh/1shg_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=1shg ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | ==See Also== | ||
*[[Spectrin|Spectrin]] | *[[Spectrin 3D structures|Spectrin 3D structures]] | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Musacchio | [[Category: Large Structures]] | ||
[[Category: Noble | [[Category: Musacchio A]] | ||
[[Category: Pauptit | [[Category: Noble M]] | ||
[[Category: Saraste | [[Category: Pauptit R]] | ||
[[Category: Wierenga | [[Category: Saraste M]] | ||
[[Category: Wierenga RK]] | |||
Latest revision as of 11:30, 14 February 2024
CRYSTAL STRUCTURE OF A SRC-HOMOLOGY 3 (SH3) DOMAINCRYSTAL STRUCTURE OF A SRC-HOMOLOGY 3 (SH3) DOMAIN
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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