1eof

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|ACTIVITY=
|ACTIVITY=
|GENE=
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|RELATEDENTRY=[[1eod|1EOD]], [[1eoe|1EOE]], [[1t1d|1T1D]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eof OCA], [http://www.ebi.ac.uk/pdbsum/1eof PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eof RCSB]</span>
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[[Category: proton transport]]
[[Category: proton transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:58:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:06:38 2008''

Revision as of 17:06, 30 March 2008


PDB ID 1eof

Drag the structure with the mouse to rotate
, resolution 2.38Å
Related: 1EOD, 1EOE, 1T1D


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE N136A MUTANT OF A SHAKER T1 DOMAIN


Overview

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

1EOF is a Single protein structure of sequence from Aplysia californica. Full crystallographic information is available from OCA.

Reference

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

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