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| | ==High resolution structure of alpha-spectrin SH3 domain mutant with a redesigned core== | | ==High resolution structure of alpha-spectrin SH3 domain mutant with a redesigned core== |
| - | <StructureSection load='3ngp' size='340' side='right' caption='[[3ngp]], [[Resolution|resolution]] 1.08Å' scene=''> | + | <StructureSection load='3ngp' size='340' side='right'caption='[[3ngp]], [[Resolution|resolution]] 1.08Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ngp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NGP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NGP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ngp]] 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=3NGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NGP FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1shg|1shg]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.084Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPTAN1, SPTA2 ([http://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'>[https://proteopedia.org/fgij/fg.htm?mol=3ngp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ngp OCA], [https://pdbe.org/3ngp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ngp RCSB], [https://www.ebi.ac.uk/pdbsum/3ngp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ngp ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ngp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ngp OCA], [http://pdbe.org/3ngp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ngp RCSB], [http://www.ebi.ac.uk/pdbsum/3ngp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ngp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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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| | ==See Also== | | ==See Also== |
| - | *[[Spectrin|Spectrin]] | + | *[[Spectrin 3D structures|Spectrin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| - | [[Category: Camara-Artigas, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Gavira, J A]] | + | [[Category: Camara-Artigas A]] |
| - | [[Category: Martin-Garcia, J M]] | + | [[Category: Gavira JA]] |
| - | [[Category: Beta barrel]]
| + | [[Category: Martin-Garcia JM]] |
| - | [[Category: Structural protein]]
| + | |
| 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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The alpha-spectrin SH3 domain (Spc-SH3) is a small modular domain which has been broadly used as a model protein in folding studies and these studies have sometimes been supported by structural information obtained from the coordinates of Spc-SH3 mutants. The structure of B5/D48G, a multiple mutant designed to improve the hydrophobic core and as a consequence the protein stability, has been solved at 1 A resolution. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a=24.79, b=37.23, c=62.95 A. This mutant also bears a D48G substitution in the distal loop and this mutation has also been reported to increase the stability of the protein by itself. The structure of the B5/D48G mutant shows a highly packed hydrophobic core and a more ordered distal loop compared with previous Spc-SH3 structures.
High-resolution structure of an alpha-spectrin SH3-domain mutant with a redesigned hydrophobic core.,Camara-Artigas A, Andujar-Sanchez M, Ortiz-Salmeron E, Cuadri C, Cobos ES, Martin-Garcia JM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt, 9):1023-7. Epub 2010 Aug 21. PMID:20823517[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Camara-Artigas A, Andujar-Sanchez M, Ortiz-Salmeron E, Cuadri C, Cobos ES, Martin-Garcia JM. High-resolution structure of an alpha-spectrin SH3-domain mutant with a redesigned hydrophobic core. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt, 9):1023-7. Epub 2010 Aug 21. PMID:20823517 doi:10.1107/S1744309110030095
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