We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2pzd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2pzd.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2pzd.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2pzd| PDB=2pzd | SCENE= }}
{{STRUCTURE_2pzd| PDB=2pzd | SCENE= }}
-
'''Crystal Structure of the HtrA2/Omi PDZ Domain Bound to a Phage-Derived Ligand (WTMFWV)'''
+
===Crystal Structure of the HtrA2/Omi PDZ Domain Bound to a Phage-Derived Ligand (WTMFWV)===
-
==Overview==
+
<!--
-
The mitochondrial serine protease HtrA2/Omi helps to maintain mitochondrial function by handling misfolded proteins in the intermembrane space. In addition, HtrA2/Omi has been implicated as a proapoptotic factor upon release into the cytoplasm during the cell death cascade. The protein contains a C-terminal PDZ domain that packs against the protease active site and inhibits proteolytic activity. Engagement of the PDZ domain by peptide ligands has been shown to activate the protease and also has been proposed to mediate substrate recognition. We report a detailed structural and functional analysis of the human HtrA2/Omi PDZ domain using peptide libraries and affinity assays to define specificity, X-ray crystallography to view molecular details of PDZ-ligand interactions, and alanine-scanning mutagenesis to probe the peptide-binding groove. We show that the HtrA2/Omi PDZ domain recognizes both C-terminal and internal stretches of extended, hydrophobic polypeptides. High-affinity ligand recognition requires contacts with up to five hydrophobic side chains by distinct sites on the PDZ domain. However, no particular residue type is absolutely required at any position, and thus, the HtrA2/Omi PDZ domain appears to be a promiscuous module adapted to recognize unstructured, hydrophobic polypeptides. This type of specificity is consistent with the biological role of HtrA2/Omi in mitochondria, which requires the recognition of diverse, exposed stretches of hydrophobic sequences in misfolded proteins. The findings are less consistent with, but do not exclude, a role for the PDZ domain in targeting the protease to specific substrates during apoptosis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17656586}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17656586 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17656586}}
==Disease==
==Disease==
Line 34: Line 38:
[[Category: Peptide-binding module]]
[[Category: Peptide-binding module]]
[[Category: Serine protease]]
[[Category: Serine protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:03:29 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:18:41 2008''

Revision as of 16:18, 27 July 2008

Template:STRUCTURE 2pzd

Contents

Crystal Structure of the HtrA2/Omi PDZ Domain Bound to a Phage-Derived Ligand (WTMFWV)

Template:ABSTRACT PUBMED 17656586

Disease

Known disease associated with this structure: Parkinson disease 13 OMIM:[606441]

About this Structure

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

Reference

Structural and functional analysis of the ligand specificity of the HtrA2/Omi PDZ domain., Zhang Y, Appleton BA, Wu P, Wiesmann C, Sidhu SS, Protein Sci. 2007 Aug;16(8):1738-50. PMID:17656586

Page seeded by OCA on Sun Jul 27 19:18:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools