4msw

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m (Protected "4msw" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4msw| PDB=4msw | SCENE= }}
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===Y78 ester mutant of KcsA in high K+===
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{{ABSTRACT_PUBMED_24128761}}
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The entry 4msw is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/KCSA_STRLI KCSA_STRLI]] Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+).<ref>PMID:7489706</ref>
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Authors: Matulef, K., Valiyaveetil, F.I.
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==About this Structure==
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[[4msw]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MSW OCA].
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Description: Y78 ester mutant of KcsA in high K+
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==Reference==
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<ref group="xtra">PMID:024128761</ref><references group="xtra"/><references/>
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[[Category: Mus musculus]]
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[[Category: Streptomyces lividans]]
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[[Category: Matulef, K.]]
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[[Category: Valiyaveetil, F I.]]
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[[Category: Channel]]
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[[Category: Ester]]
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[[Category: Membrane protein]]
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[[Category: Transport protein]]
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[[Category: Unnatural amino acid]]

Revision as of 09:37, 30 October 2013

Template:STRUCTURE 4msw

Contents

Y78 ester mutant of KcsA in high K+

Template:ABSTRACT PUBMED 24128761

Function

[KCSA_STRLI] Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+).[1]

About this Structure

4msw is a 3 chain structure with sequence from Mus musculus and Streptomyces lividans. Full crystallographic information is available from OCA.

Reference

  • Matulef K, Komarov AG, Costantino CA, Valiyaveetil FI. Using protein backbone mutagenesis to dissect the link between ion occupancy and C-type inactivation in K+ channels. Proc Natl Acad Sci U S A. 2013 Oct 15. PMID:24128761 doi:http://dx.doi.org/10.1073/pnas.1314356110
  1. ↑ Schrempf H, Schmidt O, Kummerlen R, Hinnah S, Muller D, Betzler M, Steinkamp T, Wagner R. A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBO J. 1995 Nov 1;14(21):5170-8. PMID:7489706

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