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5u6p

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Revision as of 21:51, 10 April 2020

Structure of the human HCN1 hyperpolarization-activated cyclic nucleotide-gated ion channel in complex with cAMP

5u6p, resolution 3.51Å

Structural highlights

5u6p is a 8 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	5u6o
Gene:	HCN1, BCNG1 (HUMAN)
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[HCN1_HUMAN] Early infantile epileptic encephalopathy. The disease is caused by mutations affecting the gene represented in this entry.

Function

[HCN1_HUMAN] 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). May mediate responses to sour stimuli.^[1]

Publication Abstract from PubMed

Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels underlie the control of rhythmic activity in cardiac and neuronal pacemaker cells. In HCN, the polarity of voltage dependence is uniquely reversed. Intracellular cyclic adenosine monophosphate (cAMP) levels tune the voltage response, enabling sympathetic nerve stimulation to increase the heart rate. We present cryo-electron microscopy structures of the human HCN channel in the absence and presence of cAMP at 3.5 A resolution. HCN channels contain a K+ channel selectivity filter-forming sequence from which the amino acids create a unique structure that explains Na+ and K+ permeability. The voltage sensor adopts a depolarized conformation, and the pore is closed. An S4 helix of unprecedented length extends into the cytoplasm, contacts the C-linker, and twists the inner helical gate shut. cAMP binding rotates cytoplasmic domains to favor opening of the inner helical gate. These structures advance understanding of ion selectivity, reversed polarity gating, and cAMP regulation in HCN channels.

Structures of the Human HCN1 Hyperpolarization-Activated Channel.,Lee CH, MacKinnon R Cell. 2017 Jan 12;168(1-2):111-120.e11. doi: 10.1016/j.cell.2016.12.023. Epub, 2017 Jan 12. PMID:28086084^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gill CH, Randall A, Bates SA, Hill K, Owen D, Larkman PM, Cairns W, Yusaf SP, Murdock PR, Strijbos PJ, Powell AJ, Benham CD, Davies CH. Characterization of the human HCN1 channel and its inhibition by capsazepine. Br J Pharmacol. 2004 Oct;143(3):411-21. Epub 2004 Sep 6. PMID:15351778 doi:http://dx.doi.org/10.1038/sj.bjp.0705945
↑ Lee CH, MacKinnon R. Structures of the Human HCN1 Hyperpolarization-Activated Channel. Cell. 2017 Jan 12;168(1-2):111-120.e11. doi: 10.1016/j.cell.2016.12.023. Epub, 2017 Jan 12. PMID:28086084 doi:http://dx.doi.org/10.1016/j.cell.2016.12.023

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5u6p"

@@ Line 3: / Line 3: @@
 <SX load='5u6p' size='340' side='right' viewer='molstar' caption='[[5u6p]], [[Resolution|resolution]] 3.51&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5u6p]] is a 8 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=5U6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U6P FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5u6p]] is a 8 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=5U6P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5U6P FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5u6o|5u6o]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HCN1, BCNG1 ([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=5u6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u6p OCA], [http://pdbe.org/5u6p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u6p RCSB], [http://www.ebi.ac.uk/pdbsum/5u6p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u6p ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5u6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u6p OCA], [http://pdbe.org/5u6p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u6p RCSB], [http://www.ebi.ac.uk/pdbsum/5u6p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u6p ProSAT]</span></td></tr>
 </table>
 == Disease ==

5u6p

From Proteopedia

Revision as of 21:51, 10 April 2020

Structure of the human HCN1 hyperpolarization-activated cyclic nucleotide-gated ion channel in complex with cAMP

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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