1byw: Difference between revisions

Line 1:

[[Image:1byw.~~jpg~~|left|200px]]

[[Image:1byw.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN-ERG POTASSIUM CHANNEL~~'''~~

===STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN-ERG POTASSIUM CHANNEL===

~~==Overview==~~

<!--

The ~~HERG voltage-dependent K+ channel plays a role in cardiac electrical excitability~~, ~~and when defective~~, ~~it underlies one form of~~ the ~~long QT syndrome. We have determined~~ the ~~crystal structure of the HERG K+ channel N-terminal domain and studied its role~~ as a modifier of gating using electrophysiological methods. The domain is similar in structure to a bacterial light sensor photoactive yellow protein and provides the first three-dimensional model of a eukaryotic PAS domain. Scanning mutagenesis of the domain surface has allowed the identification of a hydrophobic "hot spot" forming a putative interface with the body of the K+ channel to which it ~~tightly binds~~. ~~The presence of the domain attached to the channel slows the rate of deactivation~~. ~~Given the roles of PAS domains in biology~~, ~~we propose that~~ the ~~HERG N~~-~~terminal domain has a regulatory function.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9845367}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9845367 is the PubMed ID number.

-->

==About this Structure==

Line 27:

Line 31:

[[Category: Pas domain]]

[[Category: Potassium channel domain]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 12~~:07:58 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:58:14 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1byw.jpg|left|200px]]
+{{Seed}}
+[[Image:1byw.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1byw|  PDB=1byw  |  SCENE=  }}
-'''STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN-ERG POTASSIUM CHANNEL'''
+===STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN-ERG POTASSIUM CHANNEL===
-==Overview==
+<!--
-The HERG voltage-dependent K+ channel plays a role in cardiac electrical excitability, and when defective, it underlies one form of the long QT syndrome. We have determined the crystal structure of the HERG K+ channel N-terminal domain and studied its role as a modifier of gating using electrophysiological methods. The domain is similar in structure to a bacterial light sensor photoactive yellow protein and provides the first three-dimensional model of a eukaryotic PAS domain. Scanning mutagenesis of the domain surface has allowed the identification of a hydrophobic "hot spot" forming a putative interface with the body of the K+ channel to which it tightly binds. The presence of the domain attached to the channel slows the rate of deactivation. Given the roles of PAS domains in biology, we propose that the HERG N-terminal domain has a regulatory function.
+The line below this paragraph, {{ABSTRACT_PUBMED_9845367}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9845367 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9845367}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Pas domain]]
 [[Category: Potassium channel domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:07:58 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:58:14 2008''