2bex | pdb_00002bex
CRYSTAL STRUCTURE OF PLACENTAL RIBONUCLEASE INHIBITOR IN COMPLEX WITH HUMAN EOSINOPHIL DERIVED NEUROTOXIN AT 2A RESOLUTION
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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 [[1]], with EC number [3.1.27.5]. 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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