1OBY

Crystal structure of the complex of PDZ2 of syntenin with a syndecan-4 peptide.

Summary for 1OBY

• Entry DOI: 10.2210/pdb1oby/pdb
• Related: 1EJP 1EJQ 1NTE 1OBX 1OBZ
• Descriptor: SYNTENIN 1, SYNDECAN-4, SULFATE ION, ... (4 entities in total)
• Functional Keywords: cell adhesion, adhesion-complex, pdz domain, signal transduction, nuclear protein
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 4
• Total formula weight: 18564.91

Authors

Kang, B.S.,Cooper, D.R.,Devedjiev, Y.,Derewenda, U.,Derewenda, Z.S. (deposition date: 2003-01-31, release date: 2003-07-11, Last modification date: 2023-12-13)

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-, 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 (1.85 Å)