3etq
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3etq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ETQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ETQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[3etq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ETQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ETQ FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>< | + | </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> |
- | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q5o|1q5o]], [[1q3e|1q3e]], [[1q43|1q43]], [[2q0a|2q0a]], [[3bpz|3bpz]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q5o|1q5o]], [[1q3e|1q3e]], [[1q43|1q43]], [[2q0a|2q0a]], [[3bpz|3bpz]]</td></tr> |
- | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bcng2, Hac1, Hcn2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bcng2, Hac1, Hcn2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> |
- | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3etq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3etq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3etq RCSB], [http://www.ebi.ac.uk/pdbsum/3etq PDBsum]</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=3etq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3etq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3etq RCSB], [http://www.ebi.ac.uk/pdbsum/3etq PDBsum]</span></td></tr> |
- | <table> | + | </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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
- | [[Category: Flynn, G E | + | [[Category: Flynn, G E]] |
[[Category: Beta roll]] | [[Category: Beta roll]] | ||
[[Category: C-linker]] | [[Category: C-linker]] |
Revision as of 23:49, 24 December 2014
X-ray structure of cysteine-free fragment of mHCN2 C-terminal region from amino acids 443-630 including C508N, C584S, and C601S mutations
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Categories: Mus musculus | Flynn, G E | Beta roll | C-linker | Camp | Camp-binding | Cyclic nucleotide binding domain | Glycoprotein | Hcn | Ion channel | Ion transport | Ionic channel | Membrane | Nucleotide-binding | Phosphoprotein | Potassium | Potassium channel | Potassium transport | Sodium channel | Sodium transport | Transmembrane | Transport | Transport protein | Voltage-gated channel