6jiy: Difference between revisions

<StructureSection load='6jiy' size='340' side='right'caption='[[6jiy]], [[Resolution|resolution]] 3.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[6jiy]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JIY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JIY FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CFF:CAFFEINE'>CFF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=6jiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jiy OCA], [http://pdbe.org/6jiy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jiy RCSB], [http://www.ebi.ac.uk/pdbsum/6jiy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jiy ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/FKB1B_HUMAN FKB1B_HUMAN]] Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

The high-conductance intracellular calcium (Ca(2+)) channel RyR2 is essential for the coupling of excitation and contraction in cardiac muscle. Among various modulators, calmodulin (CaM) regulates RyR2 in a Ca(2+)-dependent manner. Here we reveal the regulatory mechanism by which porcine RyR2 is modulated by human CaM through the structural determination of RyR2 under eight conditions. Apo-CaM and Ca(2+)-CaM bind to distinct but overlapping sites in an elongated cleft formed by the handle, helical and central domains. The shift in CaM-binding sites on RyR2 is controlled by Ca(2+) binding to CaM, rather than to RyR2. Ca(2+)-CaM induces rotations and intradomain shifts of individual central domains, resulting in pore closure of the PCB95 and Ca(2+)-activated channel. By contrast, the pore of the ATP, caffeine and Ca(2+)-activated channel remains open in the presence of Ca(2+)-CaM, which suggests that Ca(2+)-CaM is one of the many competing modulators of RyR2 gating.

 

== References ==

</StructureSection>

[[Category: Chi, X M]]

[[Category: Gong, D S]]

[[Category: Huang, G X.Y]]

[[Category: Lei, J L]]

[[Category: Yan, N]]

[[Category: Zhou, G W]]

[[Category: Membrane protein]]