Crystallographic analysis of the laminin β2 short arm reveals how the LF domain is inserted into a regular array of LE domains

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Title: Crystallographic analysis of the laminin β2 short arm reveals how the LF domain is inserted into a regular array of LE domains
Authors: Pulido, D
Briggs, DC
Hua, J
Hohenester, E
Item Type: Journal Article
Abstract: Laminins are a major constituent of all basement membranes. The polymerisation of laminins at the cell surface is mediated by the three short arms of the cross-shaped laminin heterotrimer. The short arms contain repeats of laminin-type epidermal growth factor-like (LE) domains, interspersed with globular domains of unknown function. A single LF domain is inserted between LE5 and LE6 of the laminin β1 and β2 chains. We report the crystal structure at 1.85 Å resolution of the laminin β2 LE5-LF-LE6 region. The LF domain consists of a β-sandwich related to bacterial family 35 carbohydrate binding modules, and more distantly to the L4 domains present in the short arms of laminin α and γ chains. An α-helical region mediates the extensive interaction of the LF domain with LE5. The relative arrangement of LE5 and LE6 is very similar to that of consecutive LE domains in uninterrupted LE tandems. Fitting atomic models to a low-resolution structure of the first eight domains of the laminin β1 chain determined by small-angle X-ray scattering suggests a deviation from the regular LE array at the LE4-LE5 junction. These results advance our understanding of laminin structure.
Issue Date: 16-Jul-2016
Date of Acceptance: 28-Jun-2016
ISSN: 1569-1802
Publisher: Elsevier
Start Page: 204
End Page: 212
Journal / Book Title: Matrix Biology
Volume: 57-58
Copyright Statement: © 2016 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY license (
Sponsor/Funder: Imperial College Trust
Wellcome Trust
Funder's Grant Number: P48895
Keywords: Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
Cell Biology
Basement membrane
X-ray crystallography
06 Biological Sciences
Publication Status: Published
Appears in Collections:Faculty of Natural Sciences

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