5khj: Difference between revisions
New page: '''Unreleased structure''' The entry 5khj is ON HOLD Authors: Ng, L.C.T., Putrenko, I., Baronas, V., Van Petegem, F., Accili, E.A. Description: HCN2 CNBD in complex with uridine-3', 5'... |
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==HCN2 CNBD in complex with uridine-3', 5'-cyclic monophosphate (cUMP)== | |||
<StructureSection load='5khj' size='340' side='right'caption='[[5khj]], [[Resolution|resolution]] 2.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5khj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KHJ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6SY:URIDINE-3,5-CYCLIC+MONOPHOSPHATE'>6SY</scene></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=5khj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5khj OCA], [https://pdbe.org/5khj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5khj RCSB], [https://www.ebi.ac.uk/pdbsum/5khj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5khj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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> | ||
[[Category: | <div class="pdbe-citations 5khj" style="background-color:#fffaf0;"></div> | ||
[[Category: Accili | |||
[[Category: Baronas | ==See Also== | ||
[[Category: | *[[Ion channels 3D structures|Ion channels 3D structures]] | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Accili EA]] | |||
[[Category: Baronas V]] | |||
[[Category: Ng LCT]] | |||
[[Category: Putrenko I]] | |||
[[Category: Van Petegem F]] | |||
Latest revision as of 13:01, 27 September 2023
HCN2 CNBD in complex with uridine-3', 5'-cyclic monophosphate (cUMP)HCN2 CNBD in complex with uridine-3', 5'-cyclic monophosphate (cUMP)
Structural highlights
FunctionHCN2_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. See AlsoReferences
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