This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1i5h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1i5h.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1i5h.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1i5h| PDB=1i5h | SCENE= }}
{{STRUCTURE_1i5h| PDB=1i5h | SCENE= }}
-
'''SOLUTION STRUCTURE OF THE RNEDD4 WWIII DOMAIN-RENAC BP2 PEPTIDE COMPLEX'''
+
===SOLUTION STRUCTURE OF THE RNEDD4 WWIII DOMAIN-RENAC BP2 PEPTIDE COMPLEX===
-
==Overview==
+
<!--
-
Nedd4 is a ubiquitin protein ligase composed of a C2 domain, three (or four) WW domains and a ubiquitin ligase Hect domain. Nedd4 was demonstrated to bind the epithelial sodium channel (alphabetagammaENaC), by association of its WW domains with PY motifs (XPPXY) present in each ENaC subunit, and to regulate the cell surface stability of the channel. The PY motif of betaENaC is deleted or mutated in Liddle syndrome, a hereditary form of hypertension caused by elevated ENaC activity. Here we report the solution structure of the third WW domain of Nedd4 complexed to the PY motif-containing region of betaENaC (TLPIPGTPPPNYDSL, referred to as betaP2). A polyproline type II helical conformation is adopted by the PPPN sequence. Unexpectedly, the C-terminal sequence YDSL forms a helical turn and both the tyrosine and the C-terminal leucine contact the WW domain. This is unlike other proline-rich peptides complexed to WW domains, which bind in an extended conformation and lack molecular interactions with residues C-terminal to the tyrosine or the structurally equivalent residue in non-PY motif WW domain targets. The Nedd4 WW domain-ENaC betaP2 peptide structure expands our understanding of the mechanisms involved in WW domain-ligand recognition and the molecular basis of Liddle syndrome.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11323714}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11323714 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11323714}}
==About this Structure==
==About this Structure==
-
1I5H is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5H OCA].
+
1I5H is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5H OCA].
==Reference==
==Reference==
Line 32: Line 36:
[[Category: Py motif]]
[[Category: Py motif]]
[[Category: Ww domain]]
[[Category: Ww domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:35:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:27:04 2008''

Revision as of 07:27, 1 July 2008

Image:1i5h.png

Template:STRUCTURE 1i5h

SOLUTION STRUCTURE OF THE RNEDD4 WWIII DOMAIN-RENAC BP2 PEPTIDE COMPLEX

Template:ABSTRACT PUBMED 11323714

About this Structure

1I5H is a Protein complex structure of sequences from Rattus norvegicus. Full experimental information is available from OCA.

Reference

Solution structure of a Nedd4 WW domain-ENaC peptide complex., Kanelis V, Rotin D, Forman-Kay JD, Nat Struct Biol. 2001 May;8(5):407-12. PMID:11323714

Page seeded by OCA on Tue Jul 1 10:27:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i5h"
Personal tools