2zd9

<table><tr><td colspan='2'>[[2zd9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700743 Atcc 700743]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZD9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZD9 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3beh|3beh]]</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=2zd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zd9 OCA], [http://pdbe.org/2zd9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zd9 RCSB], [http://www.ebi.ac.uk/pdbsum/2zd9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zd9 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO]] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</ref>

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== Publication Abstract from PubMed ==

The six-transmembrane helix (6 TM) tetrameric cation channels form the largest ion channel family, some members of which are voltage-gated and others are not. There are no reported channel structures to match the wealth of functional data on the non-voltage-gated members. We determined the structure of the transmembrane regions of the bacterial cyclic nucleotide-regulated channel MlotiK1, a non-voltage-gated 6 TM channel. The structure showed how the S1-S4 domain and its associated linker can serve as a clamp to constrain the gate of the pore and possibly function in concert with ligand-binding domains to regulate the opening of the pore. The structure also led us to hypothesize a new mechanism by which motions of the S6 inner helices can gate the ion conduction pathway at a position along the pore closer to the selectivity filter than the canonical helix bundle crossing.

Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel.,Clayton GM, Altieri S, Heginbotham L, Unger VM, Morais-Cabral JH Proc Natl Acad Sci U S A. 2008 Feb 5;105(5):1511-5. Epub 2008 Jan 23. PMID:18216238<ref>PMID:18216238</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2zd9" style="background-color:#fffaf0;"></div>

[[Category: Atcc 700743]]

[[Category: Cabral-Morais, J M]]

[[Category: Clayton, G M]]

[[Category: Membrane protein]]

[[Category: Transmembrane protein]]