Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Victor P.T. Pau"'
Publikováno v:
Nature Structural & Molecular Biology. 24:857-865
C-type inactivation underlies important roles played by voltage-gated K+ (Kv) channels. Functional studies have provided strong evidence that a common underlying cause of this type of inactivation is an alteration near the extracellular end of the ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1d4cfaac09e80e6c70d639c88adbad0f
https://doi.org/10.1038/nsmb.3457
https://doi.org/10.1038/nsmb.3457
Autor:
Eunan Hendron, Gino Cingolani, Victor P.T. Pau, Brad S. Rothberg, Karin Abarca-Heidemann, Marc Stezzi
Publikováno v:
Biophysical Journal. 110(3)
Regulator of conductance of K+ (RCK) domains govern K+ channel and transporter activity through binding of cytosolic nucleotides or ions, although the locations and ligand-selectivities of activation sites within these domains can vary. To gain furth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df0b8f34fa399af5ee1f7fdcf2ff1bb2
Publikováno v:
The Journal of General Physiology
MthK is a Ca(2+)-gated K(+) channel whose activity is inhibited by cytoplasmic H(+). To determine possible mechanisms underlying the channel's proton sensitivity and the relation between H(+) inhibition and Ca(2+)-dependent gating, we recorded curren
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83f428067f1482be2861f9ac2ff0016b
https://doi.org/10.1085/jgp.200910387
https://doi.org/10.1085/jgp.200910387
Publikováno v:
FEBS Journal. 276:6236-6246
KcsA, a potassium channel from Streptomyces lividans, was the first ion channel to have its transmembrane domain structure determined by crystallography. Previously we have shown that its C-terminal cytoplasmic domain is crucial for the thermostabili
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fd59634caf10e19e6d3576a48e9479da
https://doi.org/10.1111/j.1742-4658.2009.07327.x
https://doi.org/10.1111/j.1742-4658.2009.07327.x
Publikováno v:
FEBS Journal. 275:6228-6236
The prokaryotic potassium channel from Streptomyces lividans, KcsA, is the first channel that has a known crystal structure of the transmembrane domain. The crystal structure of its soluble C-terminal domain, however, still remains elusive. Biophysic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::52d62d18213e041b0809e90bad34f3a5
https://doi.org/10.1111/j.1742-4658.2008.06747.x
https://doi.org/10.1111/j.1742-4658.2008.06747.x
Publikováno v:
Nature communications. 4
Ligand binding sites within proteins can interact by allosteric mechanisms to modulate binding affinities and control protein function. Here we present crystal structures of the regulator of K+ conductance (RCK) domain from a K+ channel, MthK, which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3e31811711d87d3f64e8fbebf587efe
https://pubmed.ncbi.nlm.nih.gov/24126388
https://pubmed.ncbi.nlm.nih.gov/24126388
Autor:
Karin Abarca-Heidemann, Alexander B. Taylor, Elsie Samakai, Liubov Parfenova, Brad S. Rothberg, Frank J. Smith, P. John Hart, Matthew M. Callaghan, Victor P.T. Pau
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 108(43)
Regulator of K + conductance (RCK) domains control the activity of a variety of K + transporters and channels, including the human large conductance Ca 2+ -activated K + channel that is important for blood pressure regulation and control of neuronal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77cac6bd256efbd317ce917a42f25443
https://pubmed.ncbi.nlm.nih.gov/21997217
https://pubmed.ncbi.nlm.nih.gov/21997217
Publikováno v:
The Journal of biological chemistry. 282(40)
KcsA, a potassium channel from Streptomyces lividans, is a good model for probing the general working mechanism of potassium channels. To date, the physiological activator of KcsA is still unknown, but in vitro studies showed that it could be opened
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7efa85760ac9eb0f5c3bced445bd636a
https://pubmed.ncbi.nlm.nih.gov/17693406
https://pubmed.ncbi.nlm.nih.gov/17693406
Publikováno v:
Biophysical Journal. 98(3):126a-127a
MthK is a Ca2+-gated K+ channel whose activity is modulated by cytoplasmic pH. To determine possible mechanisms underlying the channel's pH sensitivity, we recorded current through MthK channels, which were purified from E.coli membranes, reconstitut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e2acdc3056af23b518635c3c5019672
Publikováno v:
Structure. (12):2038-2047
Summary RCK domains control activity of a variety of K + channels and transporters through binding of cytoplasmic ligands. To gain insight toward mechanisms of RCK domain activation, we solved the structure of the RCK domain from the Ca 2+ -gated K +
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f535397b28f461fcc988114236e0f291