{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T05:10:44Z","timestamp":1789449044645,"version":"build-2803163510"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1998,5,15]]},"abstract":"<jats:p>Most of hereditary elliptocytosis (HE) cases are related to a spectrin dimer (SpD) self-association defect. The severity of haemolysis is correlated with the extent of the SpD self-association defect, which itself depends on the location of the mutation regarding the tetramerization site. This site is presumed to involve the first C helix of the \u03b1 chain and the last two helices, A and B, of the \u03b2 chain to reconstitute a triple helical structure (A, B and C), as observed along spectrin. Using recombinant peptides, we demonstrated that the first C helix of the \u03b1 chain and the last two helices of the \u03b2 chain alone are not sufficient to establish interactions, which only occurred when a complete triple-helical repeat was added to each partner. One adjacent repeat is necessary to stabilize the conformation of both N- and C-terminal structures directly involved in the interaction site and is sufficient to generate a binding affinity similar to that observed in the native molecule. Producing peptides carrying a \u03b2HE mutation, we reproduced the tetramerization defect as observed in patients. Therefore, the \u03b2W2024R and \u03b2W2061R mutations, which replace the invariant tryptophan and a residue located in the hydrophobic core, respectively, affect \u03b1\u2013\u03b2 interactions considerably. In contrast, the \u03b2A2013V mutation, which modifies a residue located outside any presumed interacting regions, has a minor effect on the interaction.<\/jats:p>","DOI":"10.1042\/bj3320081","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T22:02:02Z","timestamp":1439244122000},"page":"81-89","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":43,"title":["Spectrin self-association site: characterization and study of \u03b2-spectrin mutations associated with hereditary elliptocytosis"],"prefix":"10.1042","volume":"332","author":[{"given":"Ga\u00ebl","family":"NICOLAS","sequence":"first","affiliation":[{"name":"INSERM U409, Facult\u00e9 de M\u00e9decine Bichat, 75870 Paris cedex 18, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sophie","family":"PEDRONI","sequence":"additional","affiliation":[{"name":"INSERM U409, Facult\u00e9 de M\u00e9decine Bichat, 75870 Paris cedex 18, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Catherine","family":"FOURNIER","sequence":"additional","affiliation":[{"name":"INSERM U409, Facult\u00e9 de M\u00e9decine Bichat, 75870 Paris cedex 18, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huguette","family":"GAUTERO","sequence":"additional","affiliation":[{"name":"INSERM U409, Facult\u00e9 de M\u00e9decine Bichat, 75870 Paris cedex 18, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Constantin","family":"CRAESCU","sequence":"additional","affiliation":[{"name":"INSERM U350, Institut Curie, 91405 Orsay cedex, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Didier","family":"DHERMY","sequence":"additional","affiliation":[{"name":"INSERM U409, Facult\u00e9 de M\u00e9decine Bichat, 75870 Paris cedex 18, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. Christine","family":"LECOMTE","sequence":"additional","affiliation":[{"name":"INSERM U409, Facult\u00e9 de M\u00e9decine Bichat, 75870 Paris cedex 18, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/332\/1\/81\/631088\/bj3320081.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/332\/1\/81\/631088\/bj3320081.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,24]],"date-time":"2021-11-24T01:03:44Z","timestamp":1637715824000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/332\/1\/81\/37547\/Spectrin-self-association-site-characterization"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,5,15]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1998,5,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3320081","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1998,5,15]]}}}