2BEX

Crystal structure of Placental Ribonuclease Inhibitor in complex with Human Eosinophil Derived Neurotoxin at 2A resolution

Summary for 2BEX

• Entry DOI: 10.2210/pdb2bex/pdb
• Related: 1A4Y 1GQV 1HI2 1HI3 1HI4 1HI5 1K2A
• Descriptor: RIBONUCLEASE INHIBITOR, NONSECRETORY RIBONUCLEASE, GLYCEROL, ... (5 entities in total)
• Functional Keywords: hydrolase/inhibitor, complex (inhibitor-nuclease), ribonuclease inhibitor, eosinophil derived neurotoxin, rnase 2, luecine-rich repeats, protein-protein interaction, molecular recognition, hydrolase-inhibitor complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm: P13489; Lysosome (Probable): P10153
• Total number of polymer chains: 4
• Total formula weight: 131207.95

Authors

Iyer, S.,Holloway, D.E.,Kumar, K.,Shapiro, R.,Acharya, K.R. (deposition date: 2004-12-01, release date: 2005-03-17, Last modification date: 2024-11-13)

Primary citation

Iyer, S.,Holloway, D.E.,Kumar, K.,Shapiro, R.,Acharya, K.R.
Molecular Recognition of Human Eosinophil-Derived Neurotoxin (Rnase 2) by Placental Ribonuclease Inhibitor
J.Mol.Biol., 347:637-, 2005

PubMed Abstract: Placental ribonuclease inhibitor (RI) binds diverse mammalian RNases with dissociation constants that are in the femtomolar range. Previous studies on the complexes of RI with RNase A and angiogenin revealed that RI utilises largely distinctive interactions to achieve high affinity for these two ligands. Here we report a 2.0 angstroms resolution crystal structure of RI in complex with a third ligand, eosinophil-derived neurotoxin (EDN), and a mutational analysis based on this structure. The RI-EDN interface is more extensive than those of the other two complexes and contains a considerably larger set of interactions. Few of the contacts present in the RI-angiogenin complex are replicated; the correspondence to the RI-RNase A complex is somewhat greater, but still modest. The energetic contributions of various interface regions differ strikingly from those in the earlier complexes. These findings provide insight into the structural basis for the unusual combination of high avidity and relaxed stringency that RI displays.

PubMed: 15755456
DOI: 10.1016/J.JMB.2005.01.035

Experimental method

X-RAY DIFFRACTION (1.99 Å)