2byg: Difference between revisions

Revision as of 16:52, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2byg.png

Template:STRUCTURE 2byg

2ND PDZ DOMAIN OF DISCS LARGE HOMOLOGUE 22ND PDZ DOMAIN OF DISCS LARGE HOMOLOGUE 2

Template:ABSTRACT PUBMED 17384233

About this StructureAbout this Structure

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

ReferenceReference

Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions., Elkins JM, Papagrigoriou E, Berridge G, Yang X, Phillips C, Gileadi C, Savitsky P, Doyle DA, Protein Sci. 2007 Apr;16(4):683-94. PMID:17384233

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OCA

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-'''2ND PDZ DOMAIN OF DISCS LARGE HOMOLOGUE 2'''
+===2ND PDZ DOMAIN OF DISCS LARGE HOMOLOGUE 2===
-==Overview==
+<!--
-PDZ domains are protein-protein interaction modules that generally bind to the C termini of their target proteins. The C-terminal four amino acids of a prospective binding partner of a PDZ domain are typically the determinants of binding specificity. In an effort to determine the structures of a number of PDZ domains we have included appropriate four residue extensions on the C termini of PDZ domain truncation mutants, designed for self-binding. Multiple truncations of each PDZ domain were generated. The four residue extensions, which represent known specificity sequences of the target PDZ domains and cover both class I and II motifs, form intermolecular contacts in the expected manner for the interactions of PDZ domains with protein C termini for both classes. We present the structures of eight unique PDZ domains crystallized using this approach and focus on four which provide information on selectivity (PICK1 and the third PDZ domain of DLG2), binding site flexibility (the third PDZ domain of MPDZ), and peptide-domain interactions (MPDZ 12th PDZ domain). Analysis of our results shows a clear improvement in the chances of obtaining PDZ domain crystals by using this approach compared to similar truncations of the PDZ domains without the C-terminal four residue extensions.
+The line below this paragraph, {{ABSTRACT_PUBMED_17384233}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17384233}}
 ==About this Structure==
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 [[Category: Structural genomic]]
 [[Category: Structural genomics consortium]]
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