1qjt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qjt.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1qjt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qjt| PDB=1qjt | SCENE= }}
{{STRUCTURE_1qjt| PDB=1qjt | SCENE= }}
-
'''SOLUTION STRUCTURE OF THE APO EH1 DOMAIN OF MOUSE EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15, EPS15'''
+
===SOLUTION STRUCTURE OF THE APO EH1 DOMAIN OF MOUSE EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15, EPS15===
-
==Overview==
+
<!--
-
The Eps15 homology (EH) domain is a protein-protein interaction module that binds to proteins containing the asparagine-proline-phenylalanine (NPF) or tryptophan/phenylalanine-tryptophan (W/FW) motif. EH domain-containing proteins serve important roles in signaling and processes connected to transport, protein sorting, and organization of subcellular structure. Here, we report the solution structure of the apo form of the EH1 domain of mouse Eps15, as determined by high-resolution multidimensional heteronuclear NMR spectroscopy. The polypeptide folds into six alpha-helices and a short antiparallel beta-sheet. Additionally, it contains a long, structured, topologically unique C-terminal loop. Helices 2-5 form two EF-hand motifs. Structural similarity and Ca(2+) binding properties lead to classification of the EH1 domain as a member of the S100 subclass of EF-hand-containing proteins, albeit with a unique set of interhelical angles. Binding studies using an eight-residue NPF-containing peptide derived from RAB, the cellular cofactor of the HIV Rev protein, show a hydrophobic peptide-binding pocket formed by conserved tryptophan and leucine residues.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10471276}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10471276 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10471276}}
==About this Structure==
==About this Structure==
-
1QJT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJT OCA].
+
1QJT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJT OCA].
==Reference==
==Reference==
Line 32: Line 36:
[[Category: S100 protein]]
[[Category: S100 protein]]
[[Category: Solution structure]]
[[Category: Solution structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:21:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:50:07 2008''

Revision as of 20:50, 27 July 2008

Template:STRUCTURE 1qjt

SOLUTION STRUCTURE OF THE APO EH1 DOMAIN OF MOUSE EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15, EPS15

Template:ABSTRACT PUBMED 10471276

About this Structure

1QJT is a Single protein structure of sequence from Mus musculus. Full experimental information is available from OCA.

Reference

The EH1 domain of Eps15 is structurally classified as a member of the S100 subclass of EF-hand-containing proteins., Whitehead B, Tessari M, Carotenuto A, van Bergen en Henegouwen PM, Vuister GW, Biochemistry. 1999 Aug 31;38(35):11271-7. PMID:10471276

Page seeded by OCA on Sun Jul 27 23:50:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools