1eof: Difference between revisions
New page: left|200px<br /><applet load="1eof" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eof, resolution 2.38Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1eof.jpg|left|200px]]<br /><applet load="1eof" size=" | [[Image:1eof.jpg|left|200px]]<br /><applet load="1eof" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1eof, resolution 2.38Å" /> | caption="1eof, resolution 2.38Å" /> | ||
'''CRYSTAL STRUCTURE OF THE N136A MUTANT OF A SHAKER T1 DOMAIN'''<br /> | '''CRYSTAL STRUCTURE OF THE N136A MUTANT OF A SHAKER T1 DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
The T1 domain, a highly conserved cytoplasmic portion at the N-terminus of | The T1 domain, a highly conserved cytoplasmic portion at the N-terminus of the voltage-dependent K+ channel (Kv) alpha-subunit, is responsible for driving and regulating the tetramerization of the alpha-subunits. Here we report the identification of a set of mutations in the T1 domain that alter the gating properties of the Kv channel. Two mutants produce a leftward shift in the activation curve and slow the channel closing rate while a third mutation produces a rightward shift in the activation curve and speeds the channel closing rate. We have determined the crystal structures of T1 domains containing these mutations. Both of the leftward shifting mutants produce similar conformational changes in the putative membrane facing surface of the T1 domain. These results suggest that the structure of the T1 domain in this region is tightly coupled to the channel's gating states. | ||
==About this Structure== | ==About this Structure== | ||
1EOF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica]. Full crystallographic information is available from [http:// | 1EOF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOF OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Choe, S.]] | [[Category: Choe, S.]] | ||
[[Category: Cushman, S | [[Category: Cushman, S J.]] | ||
[[Category: DeRubeis, D.]] | [[Category: DeRubeis, D.]] | ||
[[Category: Jahng, A | [[Category: Jahng, A W.]] | ||
[[Category: Nanao, M | [[Category: Nanao, M H.]] | ||
[[Category: Pfaffinger, P | [[Category: Pfaffinger, P J.]] | ||
[[Category: aplysia kv1 | [[Category: aplysia kv1 1]] | ||
[[Category: potassium channels]] | [[Category: potassium channels]] | ||
[[Category: proton transport]] | [[Category: proton transport]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:54 2008'' | ||
Revision as of 13:29, 21 February 2008
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CRYSTAL STRUCTURE OF THE N136A MUTANT OF A SHAKER T1 DOMAIN
OverviewOverview
The T1 domain, a highly conserved cytoplasmic portion at the N-terminus of the voltage-dependent K+ channel (Kv) alpha-subunit, is responsible for driving and regulating the tetramerization of the alpha-subunits. Here we report the identification of a set of mutations in the T1 domain that alter the gating properties of the Kv channel. Two mutants produce a leftward shift in the activation curve and slow the channel closing rate while a third mutation produces a rightward shift in the activation curve and speeds the channel closing rate. We have determined the crystal structures of T1 domains containing these mutations. Both of the leftward shifting mutants produce similar conformational changes in the putative membrane facing surface of the T1 domain. These results suggest that the structure of the T1 domain in this region is tightly coupled to the channel's gating states.
About this StructureAbout this Structure
1EOF is a Single protein structure of sequence from Aplysia californica. Full crystallographic information is available from OCA.
ReferenceReference
Voltage dependent activation of potassium channels is coupled to T1 domain structure., Cushman SJ, Nanao MH, Jahng AW, DeRubeis D, Choe S, Pfaffinger PJ, Nat Struct Biol. 2000 May;7(5):403-7. PMID:10802739
Page seeded by OCA on Thu Feb 21 12:29:54 2008