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==Inhibitor-bound Ca2+ ATPase== | |||
=== | <StructureSection load='4j2t' size='340' side='right' caption='[[4j2t]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4j2t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J2T FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1HT:(3S,3AR,4S,6S,6AR,7S,8S,9BS)-6-(ACETYLOXY)-3A,4-BIS(BUTANOYLOXY)-3-HYDROXY-3,6,9-TRIMETHYL-8-{[(2E)-2-METHYLBUT-2-ENOYL]OXY}-2-OXO-2,3,3A,4,5,6,6A,7,8,9B-DECAHYDROAZULENO[4,5-B]FURAN-7-YL+OCTANOATE'>1HT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nal|3nal]], [[3nan|3nan]], [[3nam|3nam]], [[2c8k|2c8k]], [[3n5k|3n5k]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] </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=4j2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j2t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j2t RCSB], [http://www.ebi.ac.uk/pdbsum/4j2t PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A crystal structure suggests four water molecules are present in the binding cavity of thapsigargin in sarco/endoplasmic reticulum calcium ATPase (SERCA). Computational chemistry indicates that three of these water molecules mediate an extensive hydrogen-bonding network between thapsigargin and the backbone of SERCA. The orientation of the thapsigargin molecule in SERCA is crucially dependent on these interactions. The hypothesis has been verified by measuring the affinity of newly synthesized model compounds, which are prevented from participating in such water-mediated interactions as hydrogen-bond donors. | |||
Water-mediated interactions influence the binding of thapsigargin to sarco/endoplasmic reticulum calcium adenosinetriphosphatase.,Paulsen ES, Villadsen J, Tenori E, Liu H, Bonde DF, Lie MA, Bublitz M, Olesen C, Autzen HE, Dach I, Sehgal P, Nissen P, Moller JV, Schiott B, Christensen SB J Med Chem. 2013 May 9;56(9):3609-19. doi: 10.1021/jm4001083. Epub 2013 Apr 30. PMID:23574308<ref>PMID:23574308</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Calcium-transporting ATPase]] | [[Category: Calcium-transporting ATPase]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Autzen, H E | [[Category: Autzen, H E]] | ||
[[Category: Bonde, D F | [[Category: Bonde, D F]] | ||
[[Category: Bublitz, M | [[Category: Bublitz, M]] | ||
[[Category: Christensen, S B | [[Category: Christensen, S B]] | ||
[[Category: Dach, I | [[Category: Dach, I]] | ||
[[Category: Lie, M A | [[Category: Lie, M A]] | ||
[[Category: Liu, H | [[Category: Liu, H]] | ||
[[Category: Moller, J V | [[Category: Moller, J V]] | ||
[[Category: Nissen, P | [[Category: Nissen, P]] | ||
[[Category: Olesen, C | [[Category: Olesen, C]] | ||
[[Category: Paulsen, E S | [[Category: Paulsen, E S]] | ||
[[Category: Schiott, B | [[Category: Schiott, B]] | ||
[[Category: Sehgal, P]] | [[Category: Sehgal, P]] | ||
[[Category: Tenori, E | [[Category: Tenori, E]] | ||
[[Category: Villadsen, J | [[Category: Villadsen, J]] | ||
[[Category: Calcium transport]] | [[Category: Calcium transport]] | ||
[[Category: Hydrolase-hydrolase inhibitor complex]] | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
[[Category: P-type atpase]] | [[Category: P-type atpase]] | ||
[[Category: Thapsigargin analog]] | [[Category: Thapsigargin analog]] | ||
Revision as of 17:11, 5 January 2015
Inhibitor-bound Ca2+ ATPaseInhibitor-bound Ca2+ ATPase
Structural highlights
Publication Abstract from PubMedA crystal structure suggests four water molecules are present in the binding cavity of thapsigargin in sarco/endoplasmic reticulum calcium ATPase (SERCA). Computational chemistry indicates that three of these water molecules mediate an extensive hydrogen-bonding network between thapsigargin and the backbone of SERCA. The orientation of the thapsigargin molecule in SERCA is crucially dependent on these interactions. The hypothesis has been verified by measuring the affinity of newly synthesized model compounds, which are prevented from participating in such water-mediated interactions as hydrogen-bond donors. Water-mediated interactions influence the binding of thapsigargin to sarco/endoplasmic reticulum calcium adenosinetriphosphatase.,Paulsen ES, Villadsen J, Tenori E, Liu H, Bonde DF, Lie MA, Bublitz M, Olesen C, Autzen HE, Dach I, Sehgal P, Nissen P, Moller JV, Schiott B, Christensen SB J Med Chem. 2013 May 9;56(9):3609-19. doi: 10.1021/jm4001083. Epub 2013 Apr 30. PMID:23574308[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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