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| | <StructureSection load='1h8k' size='340' side='right'caption='[[1h8k]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1h8k' size='340' side='right'caption='[[1h8k]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1h8k]] 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=1H8K OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1H8K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1h8k]] 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=1H8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H8K FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aey|1aey]], [[1aj3|1aj3]], [[1bk2|1bk2]], [[1cun|1cun]], [[1e6g|1e6g]], [[1e6h|1e6h]], [[1e7o|1e7o]], [[1g2b|1g2b]], [[1hd3|1hd3]], [[1pwt|1pwt]], [[1qkx|1qkx]], [[1shg|1shg]], [[1tuc|1tuc]], [[1tud|1tud]]</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]] 2.7Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1h8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h8k OCA], [http://pdbe.org/1h8k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h8k RCSB], [http://www.ebi.ac.uk/pdbsum/1h8k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h8k 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=1h8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h8k OCA], [https://pdbe.org/1h8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h8k RCSB], [https://www.ebi.ac.uk/pdbsum/1h8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h8k ProSAT]</span></td></tr> |
| | </table> | | </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 == | | == 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: Serrano, L]] | + | [[Category: Serrano L]] |
| - | [[Category: Vega, M C]] | + | [[Category: Vega MC]] |
| - | [[Category: Actin-binding]]
| + | |
| - | [[Category: Calmodulin-binding]]
| + | |
| - | [[Category: Cytoskeleton]]
| + | |
| - | [[Category: Sh3-domain]]
| + | |
| 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
We have designed de novo 13 divergent spectrin SH3 core sequences to determine their folding properties. Kinetic analysis of the variants with stability similar to that of the wild type protein shows accelerated unfolding and refolding rates compatible with a preferential stabilization of the transition state. This is most likely caused by conformational strain in the native state, as deletion of a methyl group (Ile-->Val) leads to deceleration in unfolding and increased stability (up to 2 kcal x mol(-1)). Several of these Ile-->Val mutants have negative phi(-U) values, indicating that some noncanonical phi(-U) values might result from conformational strain. Thus, producing a stable protein does not necessarily mean that the design process has been entirely successful. Strained interactions could have been introduced, and a reduction in the buried volume could result in a large increase in stability and a reduction in unfolding rates.
Conformational strain in the hydrophobic core and its implications for protein folding and design.,Ventura S, Vega MC, Lacroix E, Angrand I, Spagnolo L, Serrano L Nat Struct Biol. 2002 Jun;9(6):485-93. PMID:12006985[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ventura S, Vega MC, Lacroix E, Angrand I, Spagnolo L, Serrano L. Conformational strain in the hydrophobic core and its implications for protein folding and design. Nat Struct Biol. 2002 Jun;9(6):485-93. PMID:12006985 doi:10.1038/nsb799
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