3pdz
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(New page: 200px<br /> <applet load="3pdz" size="450" color="white" frame="true" align="right" spinBox="true" caption="3pdz" /> '''SOLUTION STRUCTURE OF THE PDZ2 DOMAIN FROM ...)
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Revision as of 21:43, 12 November 2007
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SOLUTION STRUCTURE OF THE PDZ2 DOMAIN FROM HUMAN PHOSPHATASE HPTP1E
Overview
The solution structure of the second PDZ domain (PDZ2) from human, phosphatase hPTP1E has been determined using 2D and 3D heteronuclear NMR, experiments. The binding of peptides derived from the C-terminus of the, Fas receptor to PDZ2 was studied via changes in backbone peptide and, protein resonances. The structure is based on a total of 1387 nonredundant, experimental NMR restraints including 1261 interproton distance, restraints, 45 backbone hydrogen bonds, and 81 torsion angle restraints., Analysis of 30 lowest-energy structures resulted in rmsd values of 0.41, +/- 0.09 A for backbone atoms (N, Calpha, C') and 1.08 +/- 0.10 A for all, heavy atoms, excluding the disordered N- and C-termini. The hPTP1E PDZ2, structure is similar to known PDZ domain structures but contains two, unique structural features. In the peptide binding domain, the first, glycine of the GLGF motif is replaced by a serine. This serine appears to, replace a bound water observed in PDZ crystal structures that hydrogen, bonds to the bound peptide's C-terminus. The hPTP1E PDZ2 structure also, contains an unusually large loop following strand beta2 and proximal to, the peptide binding site. This well-ordered loop folds back against the, PDZ domain and contains several residues that undergo large amide chemical, shift changes upon peptide binding. Direct observation of peptide, resonances demonstrates that as many as six Fas peptide residues interact, with the PDZ2 domain.
About this Structure
3PDZ is a Single protein structure of sequence from Homo sapiens. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
Reference
Solution structure of the PDZ2 domain from human phosphatase hPTP1E and its interactions with C-terminal peptides from the Fas receptor., Kozlov G, Gehring K, Ekiel I, Biochemistry. 2000 Mar 14;39(10):2572-80. PMID:10704206
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