5k89
From Proteopedia
(Difference between revisions)
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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. 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 [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> |
</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='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> | ||
+ | <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='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'>[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> | ||
</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. | [[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. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:28368280</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 5k89" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[S100 protein|S100 protein]] | *[[S100 protein|S100 protein]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Human]] | ||
[[Category: Aligholizadeh, E]] | [[Category: Aligholizadeh, E]] | ||
[[Category: McKnight, L E]] | [[Category: McKnight, L E]] |
Revision as of 05:45, 16 May 2018
Crystal Structure of Human Calcium-Bound S100A1
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Categories: Human | Aligholizadeh, E | McKnight, L E | Melville, Z | Pozharski, E | Weber, D | Weber, D J | Calcium | Metal binding protein | S100 | S100a1