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| {{STRUCTURE_2bex| PDB=2bex | SCENE= }} | | {{STRUCTURE_2bex| PDB=2bex | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF PLACENTAL RIBONUCLEASE INHIBITOR IN COMPLEX WITH HUMAN EOSINOPHIL DERIVED NEUROTOXIN AT 2A RESOLUTION'''
| | ===CRYSTAL STRUCTURE OF PLACENTAL RIBONUCLEASE INHIBITOR IN COMPLEX WITH HUMAN EOSINOPHIL DERIVED NEUROTOXIN AT 2A RESOLUTION=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15755456}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15755456 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15755456}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rnase 2]] | | [[Category: Rnase 2]] |
| [[Category: X-ray crystallography]] | | [[Category: X-ray crystallography]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:11:58 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:36:10 2008'' |
