1D5G

SOLUTION STRUCTURE OF THE PDZ2 DOMAIN FROM HUMAN PHOSPHATASE HPTP1E COMPLEXED WITH A PEPTIDE

Summary for 1D5G

• Entry DOI: 10.2210/pdb1d5g/pdb
• Related: 3PDZ
• NMR Information: BMRB: 4516
• Descriptor: HUMAN PHOSPHATASE HPTP1E, PEPTIDE FADSEADENEQVSAV (2 entities in total)
• Functional Keywords: protein-peptide complex, hydrolase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm, cytoskeleton (By similarity): Q12923
• Total number of polymer chains: 2
• Total formula weight: 11630.84

Authors

Kozlov, G.,Gehring, K.,Ekiel, I. (deposition date: 1999-10-07, release date: 2002-07-24, Last modification date: 2024-05-22)

Primary citation

Kozlov, G.,Banville, D.,Gehring, K.,Ekiel, I.
Solution Structure of the PDZ2 Domain from Cytosolic Human Phosphatase hPTP1E Complexed with a Peptide Reveals Contribution of the beta2-beta3 Loop to PDZ Domain-Ligand Interactions
J.Mol.Biol., 320:813-820, 2002

PubMed Abstract: The solution structure of the second PDZ domain from human phosphatase hPTP1E in complex with a C-terminal peptide from the guanine nucleotide exchange factor RA-GEF-2 has been determined using 2D and 3D heteronuclear NMR experiments. Compared to previously solved structures, the hPTP1E complex shows an enlarged interaction surface with the C terminus of the bound peptide. Novel contacts were found between the long structured beta2/beta3 loop of the PDZ domain and the sixth amino acid residue from the C terminus of the peptide. This work underlines the importance of the beta2/beta3 loop for ligand selection by PDZ domains.

PubMed: 12095257
DOI: 10.1016/S0022-2836(02)00544-2

Experimental method

SOLUTION NMR