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1qrq
From Proteopedia
| 1qrq, resolution 2.80Å () | |||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
STRUCTURE OF A VOLTAGE-DEPENDENT K+ CHANNEL BETA SUBUNIT
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1qrq is a 4 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
See Also
Reference
- Gulbis JM, Mann S, MacKinnon R. Structure of a voltage-dependent K+ channel beta subunit. Cell. 1999 Jun 25;97(7):943-52. PMID:10399921
