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| | <StructureSection load='5k89' size='340' side='right'caption='[[5k89]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='5k89' size='340' side='right'caption='[[5k89]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5k89]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K89 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5k89]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K89 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 2.249Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S100A1, S100A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=5k89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k89 OCA], [http://pdbe.org/5k89 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k89 RCSB], [http://www.ebi.ac.uk/pdbsum/5k89 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k89 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=5k89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k89 OCA], [https://pdbe.org/5k89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k89 RCSB], [https://www.ebi.ac.uk/pdbsum/5k89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k89 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[S100 protein|S100 protein]] | + | *[[S100 proteins 3D structures|S100 proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aligholizadeh, E]] | + | [[Category: Aligholizadeh E]] |
| - | [[Category: McKnight, L E]] | + | [[Category: McKnight LE]] |
| - | [[Category: Melville, Z]] | + | [[Category: Melville Z]] |
| - | [[Category: Pozharski, E]] | + | [[Category: Pozharski E]] |
| - | [[Category: Weber, D]] | + | [[Category: Weber D]] |
| - | [[Category: Weber, D J]] | + | [[Category: Weber DJ]] |
| - | [[Category: Calcium]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: S100]]
| + | |
| - | [[Category: S100a1]]
| + | |
| Structural highlights
Function
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.
Publication Abstract from PubMed
S100A1 is a member of the S100 family of Ca(2+)-binding proteins and regulates several cellular processes, including those involved in Ca(2+) signaling and cardiac and skeletal muscle function. In Alzheimer's disease, brain S100A1 is overexpressed and gives rise to disease pathologies, making it a potential therapeutic target. The 2.25 A resolution crystal structure of Ca(2+)-S100A1 is solved here and is compared with the structures of other S100 proteins, most notably S100B, which is a highly homologous S100-family member that is implicated in the progression of malignant melanoma. The observed structural differences in S100A1 versus S100B provide insights regarding target protein-binding specificity and for targeting these two S100 proteins in human diseases using structure-based drug-design approaches.
X-ray crystal structure of human calcium-bound S100A1.,Melville Z, Aligholizadeh E, McKnight LE, Weber DJ, Pozharski E, Weber DJ Acta Crystallogr F Struct Biol Commun. 2017 Apr 1;73(Pt 4):215-221. doi:, 10.1107/S2053230X17003983. Epub 2017 Mar 22. PMID:28368280[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Melville Z, Aligholizadeh E, McKnight LE, Weber DJ, Pozharski E, Weber DJ. X-ray crystal structure of human calcium-bound S100A1. Acta Crystallogr F Struct Biol Commun. 2017 Apr 1;73(Pt 4):215-221. doi:, 10.1107/S2053230X17003983. Epub 2017 Mar 22. PMID:28368280 doi:http://dx.doi.org/10.1107/S2053230X17003983
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