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.


2p3w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2p3w.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2p3w.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2p3w| PDB=2p3w | SCENE= }}
{{STRUCTURE_2p3w| PDB=2p3w | SCENE= }}
-
'''Crystal Structure of the HtrA3 PDZ Domain Bound to a Phage-Derived Ligand (FGRWV)'''
+
===Crystal Structure of the HtrA3 PDZ Domain Bound to a Phage-Derived Ligand (FGRWV)===
-
==Overview==
+
<!--
-
High-temperature requirement A (HtrA) and its homologs contain a serine protease domain followed by one or two PDZ domains. Bacterial HtrA proteins and the mitochondrial protein HtrA2/Omi maintain cell function by acting as both molecular chaperones and proteases to manage misfolded proteins. The biological roles of the mammalian family members HtrA1 and HtrA3 are less clear. We report a detailed structural and functional analysis of the PDZ domains of human HtrA1 and HtrA3 using peptide libraries and affinity assays to define specificity, structural studies to view the molecular details of ligand recognition, and alanine scanning mutagenesis to investigate the energetic contributions of individual residues to ligand binding. In common with HtrA2/Omi, we show that the PDZ domains of HtrA1 and HtrA3 recognize hydrophobic polypeptides, and while C-terminal sequences are preferred, internal sequences are also recognized. However, the details of the interactions differ, as different domains rely on interactions with different residues within the ligand to achieve high affinity binding. The results suggest that mammalian HtrA PDZ domains interact with a broad range of hydrophobic binding partners. This promiscuous specificity resembles that of bacterial HtrA family members and suggests a similar function for recognizing misfolded polypeptides with exposed hydrophobic sequences. Our results support a common activation mechanism for the HtrA family, whereby hydrophobic peptides bind to the PDZ domain and induce conformational changes that activate the protease. Such a mechanism is well suited to proteases evolved for the recognition and degradation of misfolded proteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17962403}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17962403 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17962403}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Phage derived high affinity ligand]]
[[Category: Phage derived high affinity ligand]]
[[Category: Protein binding]]
[[Category: Protein binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:17:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:22:14 2008''

Revision as of 10:22, 27 July 2008

Image:2p3w.png

Template:STRUCTURE 2p3w

Crystal Structure of the HtrA3 PDZ Domain Bound to a Phage-Derived Ligand (FGRWV)

Template:ABSTRACT PUBMED 17962403

About this Structure

2P3W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural and functional analysis of the PDZ domains of human HtrA1 and HtrA3., Runyon ST, Zhang Y, Appleton BA, Sazinsky SL, Wu P, Pan B, Wiesmann C, Skelton NJ, Sidhu SS, Protein Sci. 2007 Nov;16(11):2454-71. PMID:17962403

Page seeded by OCA on Sun Jul 27 13:22:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2p3w"
Personal tools