4lp8

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'''Unreleased structure'''
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{{STRUCTURE_4lp8| PDB=4lp8 | SCENE= }}
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===A Novel Open-State Crystal Structure of the Prokaryotic Inward Rectifier KirBac3.1===
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The entry 4lp8 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/IRK10_MAGMG IRK10_MAGMG]] Inward rectifier potassium channel that mediates potassium uptake into the cell. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. The inward rectification may be achieved by the blockage of outward current by cytoplasmic divalent metal ions and polyamines. Complements an E.coli mutant that is defective in K(+) uptake.<ref>PMID:20876570</ref> <ref>PMID:20564790</ref> <ref>PMID:22231399</ref>
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Authors: Zubcevic, L., Bavro, V.N., Muniz, J.R.C., Schmidt, M.R., Wang, S., De Zorzi, R., Venien-Bryan, C., Sansom, M.S.P., Nichols. C.G., Tucker, S.J.
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==About this Structure==
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[[4lp8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LP8 OCA].
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Description: A Novel Open-State Crystal Structure of the Prokaryotic Inward Rectifier KirBac3.1
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Bavro, V N.]]
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[[Category: Muniz, J R.C.]]
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[[Category: Nichols, C G.]]
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[[Category: Sansom, M S.P.]]
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[[Category: Schmidt, M R.]]
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[[Category: Tucker, S J.]]
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[[Category: Venien-Bryan, C.]]
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[[Category: Wang, S.]]
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[[Category: Zorzi, R De.]]
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[[Category: Zubcevic, L.]]
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[[Category: Membrane]]
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[[Category: Metal transport]]
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[[Category: Potassium channel]]

Revision as of 13:44, 20 November 2013

Template:STRUCTURE 4lp8

Contents

A Novel Open-State Crystal Structure of the Prokaryotic Inward Rectifier KirBac3.1

Function

[IRK10_MAGMG] Inward rectifier potassium channel that mediates potassium uptake into the cell. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. The inward rectification may be achieved by the blockage of outward current by cytoplasmic divalent metal ions and polyamines. Complements an E.coli mutant that is defective in K(+) uptake.[1] [2] [3]

About this Structure

4lp8 is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  1. ↑ Paynter JJ, Andres-Enguix I, Fowler PW, Tottey S, Cheng W, Enkvetchakul D, Bavro VN, Kusakabe Y, Sansom MS, Robinson NJ, Nichols CG, Tucker SJ. Functional complementation and genetic deletion studies of KirBac channels: activatory mutations highlight gating-sensitive domains. J Biol Chem. 2010 Dec 24;285(52):40754-61. doi: 10.1074/jbc.M110.175687. Epub, 2010 Sep 28. PMID:20876570 doi:http://dx.doi.org/10.1074/jbc.M110.175687
  2. ↑ Clarke OB, Caputo AT, Hill AP, Vandenberg JI, Smith BJ, Gulbis JM. Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels. Cell. 2010 Jun 11;141(6):1018-29. PMID:20564790
  3. ↑ Bavro VN, De Zorzi R, Schmidt MR, Muniz JR, Zubcevic L, Sansom MS, Venien-Bryan C, Tucker SJ. Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating. Nat Struct Mol Biol. 2012 Jan 8;19(2):158-63. doi: 10.1038/nsmb.2208. PMID:22231399 doi:10.1038/nsmb.2208

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