Title: Structure and function of laminin: anatomy of a multidomain glycoprotein
Abstract: The FASEB JournalVolume 4, Issue 2 p. 148-160 ReviewsFree to Read Structure and function of laminin: anatomy of a multidomain glycoprotein Konrad Beck, Konrad Beck Institute for Biophysics, University, A-4040 Linz, AustriaSearch for more papers by this authorIrene Hunter, Irene Hunter Department of Biophysical Chemistry, Biocenter of the University, CH-4056 Basel, SwitzerlandSearch for more papers by this authorJürgen Engel, Jürgen Engel Department of Biophysical Chemistry, Biocenter of the University, CH-4056 Basel, SwitzerlandSearch for more papers by this author Konrad Beck, Konrad Beck Institute for Biophysics, University, A-4040 Linz, AustriaSearch for more papers by this authorIrene Hunter, Irene Hunter Department of Biophysical Chemistry, Biocenter of the University, CH-4056 Basel, SwitzerlandSearch for more papers by this authorJürgen Engel, Jürgen Engel Department of Biophysical Chemistry, Biocenter of the University, CH-4056 Basel, SwitzerlandSearch for more papers by this author First published: 01 February 1990 https://doi.org/10.1096/fasebj.4.2.2404817Citations: 594AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Abstract Laminin is a large (900 kDa) mosaic protein composed of many distinct domains with different structures and functions. Globular and rodlike domains are arranged in an extended four-armed, cruciform shape that is well suited for mediating between distant sites on cells and other components of the extracellular matrix. The α-helical coiled-coil domain of the long arm is involved in the specific assembly of the three chains (A, B1, B2, and possible variants) of laminin and is the only domain composed of multiple chains. It is terminated by a large globular domain composed of five homologous subdomains formed by the COOH-terminal part of the A chain. Sites for receptor-mediated cell attachment and promotion of neurite outgrowth reside in the terminal region of the long arm. A second cell attachment site, a cell signaling site with mitogenic action, binding sites for the closely associated glycoprotein nidogen/entactin, and regions involved in calcium-dependent aggregation are localized in the short arms. These domains, which to a large extent are composed of Cys-rich repeats with limited homology to EGF, are the most highly conserved regions in laminins of different origin. At present, most structural and functional data have been collected for a laminin expressed by a mouse tumor, which can be readily isolated in native form and dissected into functional fragments by limited proteolysis. Increasing information on laminins from different species and tissues demonstrates considerable variations of structure. Isoforms of laminin assembled from different chains are focally and transiently expressed and may serve distinct functions at early stages of development even before being laid down as major components of basement membranes.— Beck, K.; Hunter, I.; Engel, J. Structure and function on laminin: anatomy of a multidomain glycoprotein. FASEB J. 4: 148-160; 1990. Citing Literature Volume4, Issue2February 1990Pages 148-160 RelatedInformation
Publication Year: 1990
Publication Date: 1990-02-01
Language: en
Type: review
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 803
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