2EJY

Solution structure of the p55 PDZ T85C domain complexed with the glycophorin C F127C peptide

Summary for 2EJY

• Entry DOI: 10.2210/pdb2ejy/pdb
• Related: 2EV8
• Descriptor: 55 kDa erythrocyte membrane protein, Glycophorin C (2 entities in total)
• Functional Keywords: gpc, maguk, p55, pdz, membrane protein
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Peripheral membrane protein: Q00013; Cell membrane; Single-pass type III membrane protein: P04921
• Total number of polymer chains: 2
• Total formula weight: 12296.13

Authors

Kusunoki, H.,Kohno, T. (deposition date: 2007-03-22, release date: 2008-02-12, Last modification date: 2024-11-20)

Primary citation

Kusunoki, H.,Kohno, T.
Structural insight into the interaction between the p55 PDZ domain and glycophorin C
Biochem.Biophys.Res.Commun., 359:972-978, 2007

PubMed Abstract: p55, a member of the membrane-associated guanylate kinase family, includes a PDZ domain that specifically interacts with the C-terminal region of glycophorin C in the ternary complex of p55, protein 4.1 and glycophorin C. Here we present the first NMR-derived complex structure of the p55 PDZ domain and the C-terminal peptide of glycophorin C, obtained by using a threonine to cysteine (T85C) mutant of the p55 PDZ domain and a phenylalanine to cysteine (F127C) mutant of the glycophorin C peptide. Our NMR results revealed that the two designed mutant molecules retain the specific interaction manner that exists between the wild type molecules and can facilitate the structure determination by NMR, due to the stable complex formation via an intermolecular disulfide bond. The complex structure provides insight into the specific interaction of the p55 PDZ domain with the two key residues, Ile128 and Tyr126, of glycophorin C.

PubMed: 17572384
DOI: 10.1016/j.bbrc.2007.05.215

Experimental method

SOLUTION NMR