{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,1,14]],"date-time":"2025-01-14T05:12:46Z","timestamp":1736831566911,"version":"3.33.0"},"reference-count":53,"publisher":"International Union of Crystallography (IUCr)","issue":"8","license":[{"start":{"date-parts":[[2014,7,23]],"date-time":"2014-07-23T00:00:00Z","timestamp":1406073600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2014,7,23]],"date-time":"2014-07-23T00:00:00Z","timestamp":1406073600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr F Struct Biol Commun","Acta Crystallogr F","Acta Crystallogr F Struct Biol Cryst Commun","Acta Cryst F","Acta Cryst F Struct Biol Commun","Acta Cryst Sect F","Acta Cryst Sect F Struct Biol Commun","Acta Crystallogr Sect F","Acta Crystallogr Sect F Struct Biol Commun","Acta Crystallogr Sect F Struct Biol Cryst Commun"],"published-print":{"date-parts":[[2014,8,1]]},"abstract":"<jats:p>Adult haemoglobin (Hb) is made up of two \u03b1 and two \u03b2 subunits. Mutations that reduce expression of the \u03b1- or \u03b2-globin genes lead to the conditions \u03b1- or \u03b2-thalassaemia, respectively. Whilst both conditions are characterized by anaemia of variable severity, other details of their pathophysiology are different, in part owing to the greater stability of the \u03b2 chains that is conferred through \u03b2 self-association. In contrast, \u03b1 subunits interact weakly, and in the absence of stabilizing quaternary interactions the \u03b1 chain (\u03b1) is prone to haem loss and denaturation. The molecular contacts that confer weak self-association of \u03b1 have not been determined previously. Here, the first structure of an \u03b1<jats:sub>2<\/jats:sub>homodimer is reported in complex with one domain of the Hb receptor from<jats:italic>Staphylococcus aureus<\/jats:italic>. The \u03b1<jats:sub>2<\/jats:sub>dimer interface has a highly unusual, approximately linear, arrangement of four His side chains within hydrogen-bonding distance of each other. Some interactions present in the \u03b11\u03b21 dimer interface of native Hb are preserved in the \u03b1<jats:sub>2<\/jats:sub>dimer. However, a marked asymmetry is observed in the \u03b1<jats:sub>2<\/jats:sub>interface, suggesting that steric factors limit the number of stabilizing interactions that can form simultaneously across the interface.<\/jats:p>","DOI":"10.1107\/s2053230x14012175","type":"journal-article","created":{"date-parts":[[2014,7,22]],"date-time":"2014-07-22T16:40:13Z","timestamp":1406047213000},"page":"1032-1037","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":6,"title":["The structure of \u03b1-haemoglobin in complex with a haemoglobin-binding domain from<i>Staphylococcus aureus<\/i>reveals the elusive \u03b1-haemoglobin dimerization interface"],"prefix":"10.1107","volume":"70","author":[{"given":"Kaavya","family":"Krishna Kumar","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David A.","family":"Jacques","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J. 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