2bex
From Proteopedia
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==Overview== | ==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 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. | 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. | ||
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| + | ==Disease== | ||
| + | Known diseases associated with this structure: Central hypoventilation syndrome, congenital OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131242 131242]], Creutzfeldt-Jakob disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176640 176640]], Gerstmann-Straussler disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176640 176640]], Hirschsprung disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131242 131242]], Huntington disease-like 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176640 176640]], Insomnia, fatal familial OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176640 176640]], Prion disease with protracted course OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176640 176640]], Shah-Waardenburg syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131242 131242]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:02:01 2007'' |
Revision as of 18:55, 12 November 2007
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CRYSTAL STRUCTURE OF PLACENTAL RIBONUCLEASE INHIBITOR IN COMPLEX WITH HUMAN EOSINOPHIL DERIVED NEUROTOXIN AT 2A RESOLUTION
Contents |
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 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.
Disease
Known diseases associated with this structure: Central hypoventilation syndrome, congenital OMIM:[131242], Creutzfeldt-Jakob disease OMIM:[176640], Gerstmann-Straussler disease OMIM:[176640], Hirschsprung disease OMIM:[131242], Huntington disease-like 1 OMIM:[176640], Insomnia, fatal familial OMIM:[176640], Prion disease with protracted course OMIM:[176640], Shah-Waardenburg syndrome OMIM:[131242]
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
Page seeded by OCA on Mon Nov 12 21:02:01 2007
Categories: Homo sapiens | Pancreatic ribonuclease | Protein complex | Acharya, K.R. | Holloway, D.E. | Iyer, S. | Kumar, K. | Shapiro, R. | GOL | MAK | Eosinophil derived neurotoxin | Luecine-rich repeats | Molecular recognition | Protein-protein interaction | Ribonuclease inhibitor | Rnase 2 | X-ray crystallography
