2l0p
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2l0p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L0P FirstGlance]. <br> | <table><tr><td colspan='2'>[[2l0p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L0P FirstGlance]. <br> | ||
| - | </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=2l0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l0p OCA], [https://pdbe.org/2l0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l0p RCSB], [https://www.ebi.ac.uk/pdbsum/2l0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l0p 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=2l0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l0p OCA], [https://pdbe.org/2l0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l0p RCSB], [https://www.ebi.ac.uk/pdbsum/2l0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l0p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/S10A1_HUMAN S10A1_HUMAN] Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. | [https://www.uniprot.org/uniprot/S10A1_HUMAN S10A1_HUMAN] Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | S100A1 belongs to the EF-hand superfamily of calcium binding proteins. It is a representative of the S100 protein family based on amino acid sequence, three-dimensional structure, and biological function as a calcium signal transmitter. It is a homodimer of noncovalently bound subunits. S100A1, like most of other members of the S100 protein family, is a multifunctional, regulatory protein involved in a large variety of biological processes and closely associated with several human diseases. The three-dimensional structure of human apo-(i.e. calcium free)-S100A1 protein was determined by NMR spectroscopy (PDB 2L0P) and its backbone dynamics established by (15)N magnetic relaxation. Comparison of these results with the structure and backbone dynamics previously determined for bovine apo-S100A1 protein modified by disulfide formation with beta-mercaptoethanol at Cys 85 revealed that the secondary structure of both these proteins was almost identical, whereas the global structure of the latter was much more mobile than that of human apo-S100 protein. Differences between the structures of human and rat apo-S100A1 are also discussed. | ||
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| - | Solution NMR structure and dynamics of human apo-S100A1 protein.,Nowakowski M, Jaremko L, Jaremko M, Zhukov I, Belczyk A, Bierzynski A, Ejchart A J Struct Biol. 2011 May;174(2):391-9. Epub 2011 Feb 3. PMID:21296671<ref>PMID:21296671</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2l0p" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[S100 proteins 3D structures|S100 proteins 3D structures]] | *[[S100 proteins 3D structures|S100 proteins 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Solution structure of human apo-S100A1 protein by NMR spectroscopy
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