1s1g: Difference between revisions

Revision as of 04:03, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1s1g.png

Template:STRUCTURE 1s1g

Crystal Structure of Kv4.3 T1 DomainCrystal Structure of Kv4.3 T1 Domain

Template:ABSTRACT PUBMED 14980207

About this StructureAbout this Structure

1S1G is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Two N-terminal domains of Kv4 K(+) channels regulate binding to and modulation by KChIP1., Scannevin RH, Wang K, Jow F, Megules J, Kopsco DC, Edris W, Carroll KC, Lu Q, Xu W, Xu Z, Katz AH, Olland S, Lin L, Taylor M, Stahl M, Malakian K, Somers W, Mosyak L, Bowlby MR, Chanda P, Rhodes KJ, Neuron. 2004 Feb 19;41(4):587-98. PMID:14980207

Page seeded by OCA on Tue Jul 29 04:03:45 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1s1g.jpg|left|200px]]
+{{Seed}}
+[[Image:1s1g.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1s1g|  PDB=1s1g  |  SCENE=  }}
-'''Crystal Structure of Kv4.3 T1 Domain'''
+===Crystal Structure of Kv4.3 T1 Domain===
-==Overview==
+<!--
-The family of calcium binding proteins called KChIPs associates with Kv4 family K(+) channels and modulates their biophysical properties. Here, using mutagenesis and X-ray crystallography, we explore the interaction between Kv4 subunits and KChIP1. Two regions in the Kv4.2 N terminus, residues 7-11 and 71-90, are necessary for KChIP1 modulation and interaction with Kv4.2. When inserted into the Kv1.2 N terminus, residues 71-90 of Kv4.2 are also sufficient to confer association with KChIP1. To provide a structural framework for these data, we solved the crystal structures of Kv4.3N and KChIP1 individually. Taken together with the mutagenesis data, the individual structures suggest that that the Kv4 N terminus is required for stable association with KChIP1, perhaps through a hydrophobic surface interaction, and that residues 71-90 in Kv4 subunits form a contact loop that mediates the specific association of KChIPs with Kv4 subunits.
+The line below this paragraph, {{ABSTRACT_PUBMED_14980207}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14980207 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14980207}}
 ==About this Structure==
@@ Line 46: / Line 50: @@
 [[Category: T1 domain]]
 [[Category: Tetramerization domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:10:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:03:45 2008''