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.


2ag9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ag9.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2ag9.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ag9| PDB=2ag9 | SCENE= }}
{{STRUCTURE_2ag9| PDB=2ag9 | SCENE= }}
-
'''Crystal Structure of the Y137S mutant of GM2-Activator Protein'''
+
===Crystal Structure of the Y137S mutant of GM2-Activator Protein===
-
==Overview==
+
<!--
-
GM2-activator protein (GM2AP) is a lysosomal lipid transfer protein with important biological roles in ganglioside catabolism, phospholipid metabolism, and T-cell activation. Previous studies of crystal structures of GM2AP complexed with the physiological ligand GM2 and platelet activating factor (PAF) have shown binding at two specific locations within the spacious apolar pocket and an ordering effect of endogenous resident lipids. To investigate the structural basis of phospholipid binding further, GM2AP was cocrystallized with phosphatidylcholine (PC), known to interact with GM2AP. Analysis of three crystal forms revealed binding of single chain lipids and fatty acids only and surprisingly not intact PC. The regions of best defined electron density are consistent with the presence of lyso-PC and oleic acid, which constitute deacylation products of PC. Their acyl tails are in stacking contact with shorter, less well-defined stretches of electron density that may represent resident fatty acids. The GM2AP associated hydrolytic activity that generates lyso-PC was further confirmed by mass spectrometry and enzymatic assays. In addition, we report the structures of (i) mutant Y137S, assessing the role of Tyr137 in lipid transfer via the hydrophobic cleft, and (ii) apo-mouse GM2AP, revealing a hydrophobic pocket with a constricted opening. Our structural results provide new insights into the biological functions of GM2AP. The combined effect of hydrolytic and lipid transfer properties has profound implications in cellular signaling.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16216074}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16216074 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16216074}}
==Disease==
==Disease==
Line 23: Line 27:
==Reference==
==Reference==
Crystal structure analysis of phosphatidylcholine-GM2-activator product complexes: evidence for hydrolase activity., Wright CS, Mi LZ, Lee S, Rastinejad F, Biochemistry. 2005 Oct 18;44(41):13510-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16216074 16216074]
Crystal structure analysis of phosphatidylcholine-GM2-activator product complexes: evidence for hydrolase activity., Wright CS, Mi LZ, Lee S, Rastinejad F, Biochemistry. 2005 Oct 18;44(41):13510-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16216074 16216074]
 +
 +
Crystal structure of human GM2-activator protein with a novel beta-cup topology., Wright CS, Li SC, Rastinejad F, J Mol Biol. 2000 Dec 1;304(3):411-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11090283 11090283]
 +
 +
Structural analysis of lipid complexes of GM2-activator protein., Wright CS, Zhao Q, Rastinejad F, J Mol Biol. 2003 Aug 22;331(4):951-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12909021 12909021]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 29: Line 37:
[[Category: Rastinejad, F.]]
[[Category: Rastinejad, F.]]
[[Category: Wright, C S.]]
[[Category: Wright, C S.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:00:49 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:38:03 2008''

Revision as of 20:38, 28 July 2008

Image:2ag9.png

Template:STRUCTURE 2ag9

Contents

Crystal Structure of the Y137S mutant of GM2-Activator Protein

Template:ABSTRACT PUBMED 16216074

Disease

Known disease associated with this structure: GM2-gangliosidosis, AB variant OMIM:[272750]

About this Structure

2AG9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure analysis of phosphatidylcholine-GM2-activator product complexes: evidence for hydrolase activity., Wright CS, Mi LZ, Lee S, Rastinejad F, Biochemistry. 2005 Oct 18;44(41):13510-21. PMID:16216074

Crystal structure of human GM2-activator protein with a novel beta-cup topology., Wright CS, Li SC, Rastinejad F, J Mol Biol. 2000 Dec 1;304(3):411-22. PMID:11090283

Structural analysis of lipid complexes of GM2-activator protein., Wright CS, Zhao Q, Rastinejad F, J Mol Biol. 2003 Aug 22;331(4):951-64. PMID:12909021

Page seeded by OCA on Mon Jul 28 23:38:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ag9"
Personal tools