Structural highlights
Function
[KCAB2_RAT] Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
