Imperial College London
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ProfessorErhardHohenester

Faculty of Natural Sciences, Department of Life Sciences

Professor of Structural Matrix Biology
 
 
 
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e.hohenester

 
 
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Location

 

404ASir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Pulido:2016:10.1016/j.matbio.2016.06.006,
author = {Pulido, D and Briggs, DC and Hua, J and Hohenester, E},
doi = {10.1016/j.matbio.2016.06.006},
journal = {Matrix Biology},
pages = {204--212},
title = {Crystallographic analysis of the laminin β2 short arm reveals how the LF domain is inserted into a regular array of LE domains},
url = {http://dx.doi.org/10.1016/j.matbio.2016.06.006},
volume = {57-58},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Laminins are a major constituent of all basement membranes. The polymerisation oflaminins at the cell surface is mediated by the three short arms of the cross-shapedlaminin heterotrimer. The short arms contain repeats of laminin-type epidermalgrowth factor-like (LE) domains, interspersed with globular domains of unknownfunction. A single LF domain is inserted between LE5 and LE6 of the laminin β1 andβ2 chains. We report the crystal structure at 1.85 Å resolution of the laminin β2LE5-LF-LE6 region. The LF domain consists of a β-sandwich related to bacterialfamily 35 carbohydrate binding modules, and more distantly to the L4 domainspresent in the short arms of laminin α and γ chains. An α-helical region mediates theextensive interaction of the LF domain with LE5. The relative arrangement of LE5and LE6 is very similar to that of consecutive LE domains in uninterrupted LEtandems. Fitting atomic models to a low-resolution structure of the first eight domainsof the laminin β1 chain determined by small-angle X-ray scattering suggests adeviation from the regular LE array at the LE4-LE5 junction. These results advanceour understanding of laminin structure.
AU  - Pulido,D
AU  - Briggs,DC
AU  - Hua,J
AU  - Hohenester,E
DO  - 10.1016/j.matbio.2016.06.006
EP  - 212
PY  - 2016///
SN  - 1569-1802
SP  - 204
TI  - Crystallographic analysis of the laminin β2 short arm reveals how the LF domain is inserted into a regular array of LE domains
T2  - Matrix Biology
UR  - http://dx.doi.org/10.1016/j.matbio.2016.06.006
UR  - http://hdl.handle.net/10044/1/34165
VL  - 57-58
ER  -
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