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| | <StructureSection load='2oaw' size='340' side='right'caption='[[2oaw]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2oaw' size='340' side='right'caption='[[2oaw]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2oaw]] is a 4 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=2OAW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OAW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2oaw]] is a 4 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=2OAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OAW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1shg|1shg]], [[1bk2|1bk2]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=2oaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oaw OCA], [http://pdbe.org/2oaw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oaw RCSB], [http://www.ebi.ac.uk/pdbsum/2oaw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2oaw ProSAT]</span></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=2oaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oaw OCA], [https://pdbe.org/2oaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oaw RCSB], [https://www.ebi.ac.uk/pdbsum/2oaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oaw 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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Filimonov, V V]] | + | [[Category: Filimonov VV]] |
| - | [[Category: Gabdoulkhakov, A G]] | + | [[Category: Gabdoulkhakov AG]] |
| - | [[Category: Gushchina, L V]] | + | [[Category: Gushchina LV]] |
| - | [[Category: Nikonov, S V]] | + | [[Category: Nikonov SV]] |
| - | [[Category: Nikulin, A D]] | + | [[Category: Nikulin AD]] |
| - | [[Category: Serrano, L]] | + | [[Category: Serrano L]] |
| - | [[Category: Viguera, A R]] | + | [[Category: Viguera AR]] |
| - | [[Category: Chimera]]
| + | |
| - | [[Category: Sh3 domain]]
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| - | [[Category: Structural protein]]
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| 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
Bergerac-type chimeras of spectrin SH3 were designed by extending a beta-hairpin by eight amino acids so that the extension protruded from the domain body like a "nose" being exposed to the solvent. A calorimetric study of several Bergerac-SH3 variants was carried out over a wide range of pH values and protein concentrations and the three-dimensional structure of one of them, SHH, was determined. X-ray studies confirmed that the nose had a well defined beta-structure whilst the chimera formed a stable tetramer within the crystal unit because of four tightly packed noses. In the pH range of 4-7 the heat-induced unfolding of some chimeras was complex and concentration dependent, whilst at pH values below 3.5, low protein concentrations of all the chimeras studied, including SHH, seemed to obey a monomolecular two-state unfolding model. The best set of data was obtained for the SHA variant, the unfolding heat effects of which were systematically higher than those of the WT protein (about 16.4 kJ/mol at 323 K), which may be close to the upper limit of the enthalpy gain due to 10 residue beta-hairpin folding. At the same time, the chimeras with high nose stability, which, like SHH, have a hydrophobic (IVY) cluster on their surface, showed a lower apparent unfolding heat effect, much closer to that of the WT protein. The possible reasons for this difference are discussed.
Structural and thermodynamic studies of Bergerac-SH3 chimeras.,Gushchina LV, Gabdulkhakov AG, Nikonov SV, Mateo PL, Filimonov VV Biophys Chem. 2009 Feb;139(2-3):106-15. Epub 2008 Nov 9. PMID:19042078[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gushchina LV, Gabdulkhakov AG, Nikonov SV, Mateo PL, Filimonov VV. Structural and thermodynamic studies of Bergerac-SH3 chimeras. Biophys Chem. 2009 Feb;139(2-3):106-15. Epub 2008 Nov 9. PMID:19042078 doi:S0301-4622(08)00229-9
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