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==Crystal Structure of the R21D mutant of alpha-spectrin SH3 domain. Crystal obtained in ammonium sulphate at pH 6.== | ==Crystal Structure of the R21D mutant of alpha-spectrin SH3 domain. Crystal obtained in ammonium sulphate at pH 6.== | ||
<StructureSection load='3m0r' size='340' side='right' caption='[[3m0r]], [[Resolution|resolution]] 1.10Å' scene=''> | <StructureSection load='3m0r' size='340' side='right'caption='[[3m0r]], [[Resolution|resolution]] 1.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3m0r]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3m0r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M0R FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1shg|1shg]], [[3i9q|3i9q]], [[2f2w|2f2w]], [[2f2x|2f2x]], [[3m0p|3m0p]], [[3m0q|3m0q]], [[3m0s|3m0s]], [[3m0t|3m0t]], [[3m0u|3m0u]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1shg|1shg]], [[3i9q|3i9q]], [[2f2w|2f2w]], [[2f2x|2f2x]], [[3m0p|3m0p]], [[3m0q|3m0q]], [[3m0s|3m0s]], [[3m0t|3m0t]], [[3m0u|3m0u]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPTAN1, SPTA2 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPTAN1, SPTA2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3m0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0r OCA], [https://pdbe.org/3m0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m0r RCSB], [https://www.ebi.ac.uk/pdbsum/3m0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m0r 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. | ||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Chick]] | [[Category: Chick]] | ||
[[Category: Large Structures]] | |||
[[Category: Camara-Artigas, A]] | [[Category: Camara-Artigas, A]] | ||
[[Category: Gavira, J A]] | [[Category: Gavira, J A]] |
Revision as of 15:40, 13 October 2021
Crystal Structure of the R21D mutant of alpha-spectrin SH3 domain. Crystal obtained in ammonium sulphate at pH 6.Crystal Structure of the R21D mutant of alpha-spectrin SH3 domain. Crystal obtained in ammonium sulphate at pH 6.
Structural highlights
Function[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. See Also |
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