1qrq
From Proteopedia
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[[Image:1qrq.gif|left|200px]] | [[Image:1qrq.gif|left|200px]] | ||
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'''STRUCTURE OF A VOLTAGE-DEPENDENT K+ CHANNEL BETA SUBUNIT''' | '''STRUCTURE OF A VOLTAGE-DEPENDENT K+ CHANNEL BETA SUBUNIT''' | ||
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[[Category: MacKinnon, R.]] | [[Category: MacKinnon, R.]] | ||
[[Category: Mann, S.]] | [[Category: Mann, S.]] | ||
| - | [[Category: | + | [[Category: Aldo-keto reductase]] |
| - | [[Category: | + | [[Category: Metal transport]] |
| - | [[Category: | + | [[Category: Potassium channel subunit]] |
| - | [[Category: | + | [[Category: Tim barrel]] |
| - | [[Category: | + | [[Category: Voltage-dependent potassium channel]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:37:44 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:37, 3 May 2008
STRUCTURE OF A VOLTAGE-DEPENDENT K+ CHANNEL BETA SUBUNIT
Overview
The integral membrane subunits of many voltage-dependent potassium channels are associated with an additional protein known as the beta subunit. One function of beta subunits is to modify K+ channel gating. We have determined the structure of the conserved core of mammalian beta subunits by X-ray crystallography at 2.8 A resolution. Like the integral membrane component of K+ channels, beta subunits form a four-fold symmetric structure. Each subunit is an oxidoreductase enzyme complete with a nicotinamide co-factor in its active site. Several structural features of the enzyme active site, including its location with respect to the four-fold axis, imply that it may interact directly or indirectly with the K+ channel's voltage sensor. This structure suggests a mechanism for coupling membrane electrical excitability directly to chemistry of the cell.
About this Structure
1QRQ is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of a voltage-dependent K+ channel beta subunit., Gulbis JM, Mann S, MacKinnon R, Cell. 1999 Jun 25;97(7):943-52. PMID:10399921 Page seeded by OCA on Sat May 3 06:37:44 2008
