Evidence for coiled-coil alpha-helical regions in the long arm of laminin.
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.
D000818:Animals; D002942:Circular Dichroism; D006358:Hot Temperature; D007526:Isoelectric Point; D007797:Laminin; D051379:Mice; D008854:Microscopy, Electron; D008970:Molecular Weight; D010196:Pancreatic Elastase; D010446:Peptide Fragments; D011487:Protein Conformation
D007797:Laminin; D010446:Peptide Fragments; D010196:Pancreatic Elastase