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.


1ocs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ocs.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1ocs.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ocs| PDB=1ocs | SCENE= }}
{{STRUCTURE_1ocs| PDB=1ocs | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE YEAST PX-DOAMIN PROTEIN GRD19P (SORTING NEXIN3) COMPLEXED TO PHOSPHATIDYLINOSYTOL-3-PHOSPHATE.'''
+
===CRYSTAL STRUCTURE OF THE YEAST PX-DOAMIN PROTEIN GRD19P (SORTING NEXIN3) COMPLEXED TO PHOSPHATIDYLINOSYTOL-3-PHOSPHATE.===
-
==Overview==
+
<!--
-
Phox homology (PX) domains have been recently identified in a number of different proteins and are involved in various cellular functions such as vacuolar targeting and membrane protein trafficking. It was shown that these modules of about 130 amino acids specifically binding to phosphoinositides and that this interaction is crucial for their cellular function. The yeast genome contains 17 PX domain proteins. One of these, Grd19p, is involved in the localization of the late Golgi membrane proteins DPAP A and Kex2p. Grd19p consists of the PX domain with 30 extra residues at the N-terminal and is homologous to the functionally characterized human sorting nexin protein SNX3. We determined the 2.0 A crystal structure of Grd19p in the free form and in complex with d-myo-phosphatidylinositol 3-phosphate (diC4PtdIns(3)P), representing the first case of both free and ligand-bound conformations of the same PX module. The ligand occupies a well defined positively charged binding pocket at the interface between the beta-sheet and alpha-helical parts of the molecule. The structure of the free and bound protein are globally similar but show some significant differences in a region containing a polyproline peptide and a putative membrane attachment site.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14514667}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14514667 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14514667}}
==About this Structure==
==About this Structure==
Line 41: Line 45:
[[Category: Sorting nexin]]
[[Category: Sorting nexin]]
[[Category: Yeast protein]]
[[Category: Yeast protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:40:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:45:08 2008''

Revision as of 00:45, 28 July 2008

Image:1ocs.png

Template:STRUCTURE 1ocs

CRYSTAL STRUCTURE OF THE YEAST PX-DOAMIN PROTEIN GRD19P (SORTING NEXIN3) COMPLEXED TO PHOSPHATIDYLINOSYTOL-3-PHOSPHATE.

Template:ABSTRACT PUBMED 14514667

About this Structure

1OCS is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of the yeast Phox homology (PX) domain protein Grd19p complexed to phosphatidylinositol-3-phosphate., Zhou CZ, de La Sierra-Gallay IL, Quevillon-Cheruel S, Collinet B, Minard P, Blondeau K, Henckes G, Aufrere R, Leulliot N, Graille M, Sorel I, Savarin P, de la Torre F, Poupon A, Janin J, van Tilbeurgh H, J Biol Chem. 2003 Dec 12;278(50):50371-6. Epub 2003 Sep 26. PMID:14514667

Page seeded by OCA on Mon Jul 28 03:45:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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