1NTE

CRYSTAL STRUCTURE ANALYSIS OF THE SECOND PDZ DOMAIN OF SYNTENIN

Summary for 1NTE

• Entry DOI: 10.2210/pdb1nte/pdb
• Related: 1N99
• Descriptor: Syntenin 1, OXYGEN ATOM (3 entities in total)
• Functional Keywords: syntenin, pdz recognition, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell junction, focal adhesion: O00560
• Total number of polymer chains: 1
• Total formula weight: 8725.96

Authors

Kang, B.S.,Cooper, D.R.,Devedjiev, Y.,Derewenda, U.,Derewenda, Z.S. (deposition date: 2003-01-29, release date: 2003-07-15, Last modification date: 2023-08-16)

Primary citation

Kang, B.S.,Cooper, D.R.,Devedjiev, Y.,Derewenda, U.,Derewenda, Z.S.
Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm.
Structure, 11:845-853, 2003

PubMed Abstract: Crystal structures of the PDZ2 domain of the scaffolding protein syntenin, both unbound and in complexes with peptides derived from C termini of IL5 receptor (alpha chain) and syndecan, reveal the molecular roots of syntenin's degenerate specificity. Three distinct binding sites (S(0), S(-1), and S(-2)), with affinities for hydrophobic side chains, function in a combinatorial way: S(-1) and S(-2) act together to bind syndecan, while S(0) and S(-1) are involved in the binding of IL5Ralpha. Neither mode of interaction is consistent with the prior classification scheme, which defined the IL5Ralpha interaction as class I (-S/T-X-phi) and the syndecan interaction as class II (-phi-X-phi). These results, in conjunction with other emerging structural data on PDZ domains, call for a revision of their classification and of the existing model of their mechanism.

PubMed: 12842047
DOI: 10.1016/S0969-2126(03)00125-4

Experimental method

X-RAY DIFFRACTION (1.24 Å)