{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,15]],"date-time":"2026-08-15T07:23:34Z","timestamp":1786778614596,"version":"build-2736575974"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1996,3,15]]},"abstract":"<jats:p>The globular domain IVa (about 250 residues) of the laminin \u03b11 chain was obtained in recombinant form from mammalian cell clones. It was prepared either with (\u03b11IVa-R) or without (\u03b11IVa) an adjacent cell-adhesive RGD site which seems to be masked in laminin-1. The recombinant products could be visualized as globular structures by rotary shadowing, were resistant to trypsin and shared immunological epitopes with laminin-1, indicating folding into a native structure. Sequence analysis of pepsin fragments demonstrated the insertion of the globular domain into an epidermal growth factor-like scaffold which is characteristic of the extracellular laminin domain IV (L4) module. Only little immunological cross-reaction was found, however, with other L4 modules from perlecan and different laminin isoforms. Fragment \u03b11IVa-R, but not fragment \u03b11IVa, bound to \u03b1V\u03b23 integrin, although to a distinctly lower level than a laminin fragment where the RGD site is fully exposed. The fragments also had no or only little cell attachment activity. This confirmed previous predictions that the globular domain \u03b11IVa masks the RGD site in laminin-1. Domain \u03b11IVa showed, in addition, a weak binding activity for the basement-membrane protein fibulin-1.<\/jats:p>","DOI":"10.1042\/bj3140847","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:47:57Z","timestamp":1439243277000},"page":"847-851","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["Structural and functional analysis of the globular domain IVa of the laminin \u03b11 chain and its impact on an adjacent RGD site"],"prefix":"10.1042","volume":"314","author":[{"given":"Bettina","family":"SCHULZE","sequence":"first","affiliation":[{"name":"Max-Planck-Institut f\u00fcr Biochemie, D-82152 Martinsried, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karlheinz","family":"MANN","sequence":"additional","affiliation":[{"name":"Max-Planck-Institut f\u00fcr Biochemie, D-82152 Martinsried, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ernst","family":"P\u00d6SCHL","sequence":"additional","affiliation":[{"name":"Max-Planck-Institut f\u00fcr Biochemie, D-82152 Martinsried, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshihiko","family":"YAMADA","sequence":"additional","affiliation":[{"name":"National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rupert","family":"TIMPL","sequence":"additional","affiliation":[{"name":"Max-Planck-Institut f\u00fcr Biochemie, D-82152 Martinsried, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/314\/3\/847\/618738\/bj3140847.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/314\/3\/847\/618738\/bj3140847.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,24]],"date-time":"2021-11-24T01:02:31Z","timestamp":1637715751000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/314\/3\/847\/37411\/Structural-and-functional-analysis-of-the-globular"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996,3,15]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1996,3,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3140847","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1996,3,15]]}}}