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| | ==SH3-subunit of chicken alpha spectrin solved by NMR== | | ==SH3-subunit of chicken alpha spectrin solved by NMR== |
| - | <StructureSection load='6scw' size='340' side='right'caption='[[6scw]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='6scw' size='340' side='right'caption='[[6scw]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6scw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SCW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6scw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SCW FirstGlance]. <br> |
| - | </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=6scw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scw OCA], [http://pdbe.org/6scw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6scw RCSB], [http://www.ebi.ac.uk/pdbsum/6scw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6scw ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=6scw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scw OCA], [https://pdbe.org/6scw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6scw RCSB], [https://www.ebi.ac.uk/pdbsum/6scw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6scw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A480YEE4_PIG A0A480YEE4_PIG] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6scw" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6scw" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Spectrin 3D structures|Spectrin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pig]] | + | [[Category: Sus scrofa]] |
| - | [[Category: Grohe, K]] | + | [[Category: Grohe K]] |
| - | [[Category: Hebrank, C]] | + | [[Category: Hebrank C]] |
| - | [[Category: Linser, R]] | + | [[Category: Linser R]] |
| - | [[Category: Beta-barrel]]
| + | |
| - | [[Category: Binding-domain]]
| + | |
| - | [[Category: Membrane-ancor]]
| + | |
| - | [[Category: Peptide binding protein]]
| + | |
| - | [[Category: Spectrin]]
| + | |
| Structural highlights
Function
A0A480YEE4_PIG
Publication Abstract from PubMed
Proteins depend on defined molecular plasticity for their functionality. How to comprehensively capture dynamics correctly is of ubiquitous biological importance. Approaches commonly used to probe protein dynamics include model-free elucidation of site-specific motion by NMR relaxation, molecular dynamics (MD)-based approaches, and capturing the substates within a dynamic ensemble by recent eNOE-based multiple-structure approaches. Even though MD is sometimes combined with ensemble-averaged NMR restraints, these approaches have largely been developed and used individually. Owing to the different underlying concepts and practical requirements, it has remained unclear how they compare, and how they cross-validate and complement each other. Here, we extract and compare the differential information contents of MD simulations, NMR relaxation measurements, and eNOE-based multi-state structures for the SH3 domain of chicken alpha-spectrin. The data show that a validated, consistent, and detailed picture is feasible both for timescales and actual conformational states sampled in the dynamic ensemble. This includes the biologically important side-chain plasticity, for which experimentally cross-validated assessment is a significant challenge.
Protein Motional Details Revealed by Complementary Structural Biology Techniques.,Grohe K, Patel S, Hebrank C, Medina S, Klein A, Rovo P, Vasa SK, Singh H, Vogeli B, Schafer LV, Linser R Structure. 2020 Jun 22. pii: S0969-2126(20)30204-5. doi:, 10.1016/j.str.2020.06.001. PMID:32579946[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Grohe K, Patel S, Hebrank C, Medina S, Klein A, Rovo P, Vasa SK, Singh H, Vogeli B, Schafer LV, Linser R. Protein Motional Details Revealed by Complementary Structural Biology Techniques. Structure. 2020 Jun 22. pii: S0969-2126(20)30204-5. doi:, 10.1016/j.str.2020.06.001. PMID:32579946 doi:http://dx.doi.org/10.1016/j.str.2020.06.001
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