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Intensive structural and functional analyses of Ang have been paramount in assigning functions to this novel homologue of bovine pancreatic RNase A. However, inhibitor\u2010binding studies with crystalline Ang (for designing potential anti\u2010cancer drugs) have been hampered as a result of the inaccessibility of the active site. Experiments with the murine homologues of Ang have not only overcome the obvious practical limitations encountered when studying the role of a human protein in healthy individuals, but also the crystal structures of murine angiogenins (<jats:styled-content style=\"fixed-case\">mA<\/jats:styled-content>ng and <jats:styled-content style=\"fixed-case\">mA<\/jats:styled-content>ng\u20104) have revealed themselves to have greater potential for the visualization of small\u2010molecule inhibitor binding at the active site. In the present study, we report the crystal structures of two more murine Ang paralogues, <jats:styled-content style=\"fixed-case\">mA<\/jats:styled-content>ng\u20102 and <jats:styled-content style=\"fixed-case\">mA<\/jats:styled-content>ng\u20103, at 1.6 and 1.8\u00a0\u00c5 resolution, respectively. These constitute the first crystal structures of an Ang with a zinc ion bound at the active site and provide some insight into the possible mode of inhibition of the ribonucleolytic activity of the enzyme by these divalent cations. Both structures show that the residues forming the putative P<jats:sub>1<\/jats:sub>, B<jats:sub>1<\/jats:sub> and B<jats:sub>2<\/jats:sub> subsites occupy positions similar to their counterparts in human Ang and are likely to have conserved roles. However, a less obtrusive conformation of the C\u2010terminal segment in <jats:styled-content style=\"fixed-case\">mA<\/jats:styled-content>ng\u20103 and the presence of a sulfate ion in the B<jats:sub>1<\/jats:sub> subsite of <jats:styled-content style=\"fixed-case\">mA<\/jats:styled-content>ng\u20102 suggest that these proteins have the potential to be used for inhibitor\u2010binding studies. We also discuss the biological relevance of the structural similarities and differences between the different Ang homologues.<\/jats:p><\/jats:sec><jats:sec><jats:title>Database<\/jats:title><jats:p>The atomic coordinates and structure factors for <jats:styled-content style=\"fixed-case\">mA<\/jats:styled-content>ng\u20102 (<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/pdb\/search\/structidSearch.do?structureId=3ZBV\">3ZBV<\/jats:ext-link>) and <jats:styled-content style=\"fixed-case\">mA<\/jats:styled-content>ng\u20103 (<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/pdb\/search\/structidSearch.do?structureId=3ZBW\">3ZBW<\/jats:ext-link>) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ, USA (<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/\">http:\/\/www.rcsb.org\/<\/jats:ext-link>).<\/jats:p><\/jats:sec><jats:sec><jats:title>Structured digital abstract<\/jats:title><jats:p>\n<jats:list list-type=\"bullet\">\n<jats:list-item><jats:p><jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.uniprot.org\/uniprot\/P97802\">mAng2<\/jats:ext-link>\u00a0and\u00a0<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.uniprot.org\/uniprot\/P97802\">mAng3<\/jats:ext-link>\u00a0<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.ebi.ac.uk\/ontology-lookup\/?termId=MI:0407\">bind<\/jats:ext-link>\u00a0by\u00a0<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.ebi.ac.uk\/ontology-lookup\/?termId=MI:0114\">x-ray crystallography<\/jats:ext-link>\u00a0(<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/mint.bio.uniroma2.it\/mint\/search\/interaction.do?interactionAc=MINT-8402272\">View interaction<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n<\/jats:list>\n<\/jats:p><\/jats:sec>","DOI":"10.1111\/febs.12071","type":"journal-article","created":{"date-parts":[[2012,11,21]],"date-time":"2012-11-21T18:46:28Z","timestamp":1353523588000},"page":"302-318","source":"Crossref","is-referenced-by-count":9,"title":["Crystal structures of murine angiogenin\u20102 and \u20103 \u2013 probing \u2018structure \u2013 function\u2019 relationships amongst angiogenin homologues"],"prefix":"10.1111","volume":"280","author":[{"given":"Shalini","family":"Iyer","sequence":"first","affiliation":[{"name":"Department of Biology and Biochemistry University of Bath UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel E.","family":"Holloway","sequence":"additional","affiliation":[{"name":"Department of Biology and Biochemistry University of Bath UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"K. 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