5khh: Difference between revisions
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==HCN2 CNBD in complex with inosine-3', 5'-cyclic monophosphate (cIMP)== | |||
<StructureSection load='5khh' size='340' side='right' caption='[[5khh]], [[Resolution|resolution]] 1.77Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5khh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KHH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KHH FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6SW:INOSINE-3,5-CYCLIC+MONOPHOSPHATE'>6SW</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5khg|5khg]], [[5khi|5khi]], [[5khj|5khj]], [[5khk|5khk]]</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=5khh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5khh OCA], [http://pdbe.org/5khh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5khh RCSB], [http://www.ebi.ac.uk/pdbsum/5khh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5khh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/HCN2_MOUSE HCN2_MOUSE]] Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current. Activated by cAMP. Modulated by intracellular chloride ions and pH; acidic pH shifts the activation to more negative voltages.<ref>PMID:11741901</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cyclic AMP is thought to facilitate the opening of the HCN2 channel by binding to a C-terminal domain and promoting or inhibiting interactions between subunits. Here, we correlated the ability of cyclic nucleotides to promote interactions of isolated HCN2 C-terminal domains in solution with their ability to facilitate channel opening. Cyclic IMP, a cyclic purine nucleotide, and cCMP, a cyclic pyrimidine nucleotide, bind to a C-terminal domain containing the cyclic nucleotide-binding domain but, in contrast to other cyclic nucleotides examined, fail to promote its oligomerization, and produce only modest facilitation of opening of the full-length channel. Comparisons between ligand bound structures identify a region between the sixth and seventh beta strands and the distal C helix as important for facilitation and tight binding. We propose that promotion of interactions between the C-terminal domains by a given ligand contribute to its ability to facilitate opening of the full-length channel. | |||
Cyclic Purine and Pyrimidine Nucleotides Bind to the HCN2 Ion Channel and Variably Promote C-Terminal Domain Interactions and Opening.,Ng LC, Putrenko I, Baronas V, Van Petegem F, Accili EA Structure. 2016 Aug 23. pii: S0969-2126(16)30193-9. doi:, 10.1016/j.str.2016.06.024. PMID:27568927<ref>PMID:27568927</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5khh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Accili, E A]] | |||
[[Category: Baronas, V]] | |||
[[Category: Ng, L C.T]] | |||
[[Category: Petegem, F Van]] | |||
[[Category: Putrenko, I]] | [[Category: Putrenko, I]] | ||
[[Category: | [[Category: Cycilc nucleotide binding domain]] | ||
[[Category: | [[Category: Ion transport]] | ||
[[Category: | [[Category: Protein-ligand complex]] | ||
[[Category: | [[Category: Transport protein]] | ||
Revision as of 18:18, 14 September 2016
HCN2 CNBD in complex with inosine-3', 5'-cyclic monophosphate (cIMP)HCN2 CNBD in complex with inosine-3', 5'-cyclic monophosphate (cIMP)
Structural highlights
Function[HCN2_MOUSE] Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current. Activated by cAMP. Modulated by intracellular chloride ions and pH; acidic pH shifts the activation to more negative voltages.[1] Publication Abstract from PubMedCyclic AMP is thought to facilitate the opening of the HCN2 channel by binding to a C-terminal domain and promoting or inhibiting interactions between subunits. Here, we correlated the ability of cyclic nucleotides to promote interactions of isolated HCN2 C-terminal domains in solution with their ability to facilitate channel opening. Cyclic IMP, a cyclic purine nucleotide, and cCMP, a cyclic pyrimidine nucleotide, bind to a C-terminal domain containing the cyclic nucleotide-binding domain but, in contrast to other cyclic nucleotides examined, fail to promote its oligomerization, and produce only modest facilitation of opening of the full-length channel. Comparisons between ligand bound structures identify a region between the sixth and seventh beta strands and the distal C helix as important for facilitation and tight binding. We propose that promotion of interactions between the C-terminal domains by a given ligand contribute to its ability to facilitate opening of the full-length channel. Cyclic Purine and Pyrimidine Nucleotides Bind to the HCN2 Ion Channel and Variably Promote C-Terminal Domain Interactions and Opening.,Ng LC, Putrenko I, Baronas V, Van Petegem F, Accili EA Structure. 2016 Aug 23. pii: S0969-2126(16)30193-9. doi:, 10.1016/j.str.2016.06.024. PMID:27568927[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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