2bex

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Image:2bex.gif

2bex, resolution 1.99Å

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CRYSTAL STRUCTURE OF PLACENTAL RIBONUCLEASE INHIBITOR IN COMPLEX WITH HUMAN EOSINOPHIL DERIVED NEUROTOXIN AT 2A RESOLUTION

Overview

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 ... [(full description)]

About this Structure

2BEX is a [Protein complex] structure of sequences from [Homo sapiens] with MAK and GOL as [ligands]. Active as [Pancreatic ribonuclease], with EC number [3.1.27.5]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Molecular recognition of human eosinophil-derived neurotoxin (RNase 2) by placental ribonuclease inhibitor., Iyer S, Holloway DE, Kumar K, Shapiro R, Acharya KR, J Mol Biol. 2005 Apr 1;347(3):637-55. PMID:15755456

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