{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,13]],"date-time":"2026-01-13T23:41:38Z","timestamp":1768347698012,"version":"3.49.0"},"reference-count":60,"publisher":"International Union of Crystallography (IUCr)","issue":"11","license":[{"start":{"date-parts":[[2017,10,25]],"date-time":"2017-10-25T00:00:00Z","timestamp":1508889600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2017,10,25]],"date-time":"2017-10-25T00:00:00Z","timestamp":1508889600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"funder":[{"name":"National Science Center","award":["2013\/11\/B\/ST5\/02271"],"award-info":[{"award-number":["2013\/11\/B\/ST5\/02271"]}]}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr D Struct Biol","Acta Crystallogr D","Acta Cryst D","Acta Cryst D Struct Biol","Acta Cryst Sect D","Acta Cryst Sect D Struct Biol","Acta Crystallogr Sect D","Acta Crystallogr Sect D Struct Biol","Acta Crystallogr D Biol Crystallogr","Acta Cryst D Biol Cryst"],"published-print":{"date-parts":[[2017,11,1]]},"abstract":"<jats:p>Serum albumin (SA) is the most abundant protein in plasma and is the main transporter of molecules in the circulatory system of all vertebrates, with applications in medicine, the pharmaceutical industry and molecular biology. It is known that albumins from different organisms vary in sequence; thus, it is important to know the impact of the amino-acid sequence on the three-dimensional structure and ligand-binding properties. Here, crystal structures of ovine (OSA) and caprine (CSA) serum albumins, isolated from sheep and goat blood, are described, as well those of their complexes with 3,5-diiodosalicylic acid (DIS): OSA\u2013DIS (2.20\u2005\u00c5 resolution) and CSA\u2013DIS (1.78\u2005\u00c5 resolution). The ligand-free OSA structure was determined in the trigonal space group<jats:italic>P<\/jats:italic>3<jats:sub>2<\/jats:sub>21 at 2.30\u2005\u00c5 resolution, while that of CSA in the orthorhombic space group<jats:italic>P<\/jats:italic>2<jats:sub>1<\/jats:sub>2<jats:sub>1<\/jats:sub>2<jats:sub>1<\/jats:sub>was determined at 1.94\u2005\u00c5 resolution. Both albumins are also capable of crystallizing in the triclinic space group<jats:italic>P<\/jats:italic>1, giving isostructural crystals that diffract to around 2.5\u2005\u00c5 resolution. A comparison of OSA and CSA with the closely related bovine serum albumin (BSA) shows both similarities and differences in the distribution of DIS binding sites. The investigated serum albumins from domesticated ruminants in their complexes with DIS are also compared with the analogous structures of equine and human serum albumins (ESA\u2013DIS and HSA\u2013DIS). Surprisingly, despite 98% sequence similarity, OSA binds only two molecules of DIS, whereas CSA binds six molecules of this ligand. Moreover, the binding of DIS to OSA and CSA introduced changes in the overall architecture of the proteins, causing not only different conformations of the amino-acid side chains in the binding pockets, but also a significant shift of the whole helices, changing the volume of the binding cavities.<\/jats:p>","DOI":"10.1107\/s205979831701470x","type":"journal-article","created":{"date-parts":[[2017,10,25]],"date-time":"2017-10-25T13:54:44Z","timestamp":1508939684000},"page":"896-909","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":26,"title":["Crystal structures of serum albumins from domesticated ruminants and their complexes with 3,5-diiodosalicylic acid"],"prefix":"10.1107","volume":"73","author":[{"given":"Anna","family":"Bujacz","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Julita A.","family":"Talaj","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kamil","family":"Zielinski","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Agnieszka J.","family":"Pietrzyk-Brzezinska","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Piotr","family":"Neumann","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"329","published-online":{"date-parts":[[2017,10,25]]},"reference":[{"key":"dw5186_bb1","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1007\/s10969-011-9101-7","volume":"12","author":"Abendroth","year":"2011","journal-title":"J. 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