3ffq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:45, 6 September 2023) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3ffq.png|left|200px]]
 
-
{{STRUCTURE_3ffq| PDB=3ffq | SCENE= }}
+
==HCN2I 443-640 apo-state==
 +
<StructureSection load='3ffq' size='340' side='right'caption='[[3ffq]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3ffq]] 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=3FFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FFQ 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]] 2.4&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</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=3ffq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffq OCA], [https://pdbe.org/3ffq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ffq RCSB], [https://www.ebi.ac.uk/pdbsum/3ffq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffq 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>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/3ffq_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ffq ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Visualizing conformational dynamics in proteins has been difficult, and the atomic-scale motions responsible for the behavior of most allosteric proteins are unknown. Here we report that fluorescence resonance energy transfer (FRET) between a small fluorescent dye and a nickel ion bound to a dihistidine motif can be used to monitor small structural rearrangements in proteins. This method provides several key advantages over classical FRET, including the ability to measure the dynamics of close-range interactions, the use of small probes with short linkers, a low orientation dependence, and the ability to add and remove unique tunable acceptors. We used this 'transition metal ion FRET' approach along with X-ray crystallography to determine the structural changes of the gating ring of the mouse hyperpolarization-activated cyclic nucleotide-regulated ion channel HCN2. Our results suggest a general model for the conformational switch in the cyclic nucleotide-binding site of cyclic nucleotide-regulated ion channels.
-
===HCN2I 443-640 apo-state===
+
Mapping the structure and conformational movements of proteins with transition metal ion FRET.,Taraska JW, Puljung MC, Olivier NB, Flynn GE, Zagotta WN Nat Methods. 2009 Jul;6(7):532-7. Epub 2009 Jun 14. PMID:19525958<ref>PMID:19525958</ref>
-
{{ABSTRACT_PUBMED_19525958}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 3ffq" style="background-color:#fffaf0;"></div>
-
[[3ffq]] 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=3FFQ OCA].
+
==See Also==
==See Also==
-
*[[Ion channels|Ion channels]]
+
*[[Ion channels 3D structures|Ion channels 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:019525958</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Olivier, N B.]]
+
[[Category: Olivier NB]]
-
[[Category: Camp]]
+
-
[[Category: Camp-binding]]
+
-
[[Category: Glycoprotein]]
+
-
[[Category: Ion channel]]
+
-
[[Category: Ion transport]]
+
-
[[Category: Ionic channel]]
+
-
[[Category: Membrane]]
+
-
[[Category: Metal transport]]
+
-
[[Category: Nucleotide-binding]]
+
-
[[Category: Phosphoprotein]]
+
-
[[Category: Potassium]]
+
-
[[Category: Potassium channel]]
+
-
[[Category: Potassium transport]]
+
-
[[Category: Sodium channel]]
+
-
[[Category: Sodium transport]]
+
-
[[Category: Transmembrane]]
+
-
[[Category: Transport]]
+
-
[[Category: Voltage-gated channel]]
+

Current revision

HCN2I 443-640 apo-state

PDB ID 3ffq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ffq"
Personal tools