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http://purl.uniprot.org/citations/16100951http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16100951http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16100951http://www.w3.org/2000/01/rdf-schema#comment"

Background

Protein-protein recognition is fundamental to most biological processes. The information we have so far on the interfaces between proteins comes largely from several protease-inhibitor and antigen-antibody complexes. Barnase, a bacterial ribonuclease, and barstar, its natural inhibitor, form a tight complex which provides a good model for the study and design of protein-protein non-covalent interactions.

Results

Here we report the structure of a complex between barnase and a fully functional mutant of barstar determined by X-ray analysis. Barstar is composed of three parallel alpha-helices stacked against a three-stranded parallel, beta-sheet, and sterically blocks the active site of the enzyme with an alpha-helix and adjacent loop. The buried surface in the interface between the two molecules totals 1630 A2. The barnase-barstar complex is predominantly stabilized by charge interactions involving positive charges in the active site of the enzyme. Asp39 of barstar binds to the phosphate-binding site of barnase, mimicking enzyme-substrate interactions.

Conclusion

The phosphate-binding site of the enzyme is the anchor point for inhibitor binding. We propose that this is also likely to be the case for other ribonuclease inhibitors."xsd:string
http://purl.uniprot.org/citations/16100951http://purl.org/dc/terms/identifier"doi:10.1016/0969-2126(93)90018-c"xsd:string
http://purl.uniprot.org/citations/16100951http://purl.org/dc/terms/identifier"doi:10.1016/0969-2126(93)90018-c"xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/author"Guillet V."xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/author"Guillet V."xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/author"Hartley R.W."xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/author"Hartley R.W."xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/author"Lapthorn A."xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/author"Lapthorn A."xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/author"Mauguen Y."xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/author"Mauguen Y."xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/pages"165-177"xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/pages"165-177"xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/title"Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar."xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/title"Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar."xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/volume"1"xsd:string
http://purl.uniprot.org/citations/16100951http://purl.uniprot.org/core/volume"1"xsd:string
http://purl.uniprot.org/citations/16100951http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16100951
http://purl.uniprot.org/citations/16100951http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16100951
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