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PMID: 3848400 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Evidence for coiled-coil alpha-helical regions in the long arm of laminin.

The EMBO journal ·Vol. 4 ·No. 2 ·1985-02-00 ·Pages 309-16

Paulsson M, Deutzmann R, Timpl R, Dalzoppo D, Odermatt E, Engel J

Abstract

Three new laminin fragments, E8, E9 and 25K with mol. wt. 50 000-280 000, were prepared from a limited elastase digest of laminin and from tissue extracts. They were similar with respect to their rod-like structure, a high alpha-helix content, the assembly from two chain segments and immunological cross-reactivity. Two of the fragments (E8 and E9) possess in addition globular domains which lack alpha-helices. Chemical, immunological and physical data together with sequence analysis strongly indicate that the alpha-helical segments are assembled in coiled-coil structures which are located in the rod of the long arm of laminin. These data give new insights into the overall structure of the protein.

MeSH Terms
Animals Circular Dichroism Hot Temperature Isoelectric Point Laminin Mice Microscopy, Electron Molecular Weight Pancreatic Elastase Peptide Fragments Protein Conformation
Chemicals
Laminin Peptide Fragments Pancreatic Elastase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Paulsson M
Deutzmann R
Timpl R
Dalzoppo D
Odermatt E
Engel J
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33 references, click to expand
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1985-02-00
Pages
309-16
Language
English
Region
England
NLM ID
8208664
PMCID
PMC554187
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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