Structure and function of laminin LG modules

  • Timpl R
  • Tisi D
  • Talts J
 et al. 
  • 86


    Mendeley users who have this article in their library.
  • 223


    Citations of this article.


Laminin G domain-like (LG) modules of approximately 180-200 residues are found in a number of extracellular and receptor proteins and often are present in tandem arrays. LG modules are implicated in interactions with cellular receptors (integrins, α-dystroglycan), sulfated carbohydrates and other extracellular ligands. The recently determined crystal structures of LG modules of the laminin α2 chain reveal a compact β sandwich fold and identify a novel calcium binding site. Binding epitopes for heparin, sulfatides and α-dystroglycan have been mapped by site-directed mutagenesis and show considerable overlap. The epitopes are located in surface loops around the calcium site, which in other proteins (agrin, neurexins) are modified by alternative splicing. Efficient ligand binding often requires LG modules to be present in tandem. The close proximity of the N- and C-termini in the LG module, as well as a unique link region between laminin LG3 and LG4, impose certain constraints on the arrangement of LG tandems. Further modifications may be introduced by proteolytic processing of laminin G domains, which is known to occur in the α2, α3 and α4 chains. (C) 2000 Elsevier Science B.V.

Author-supplied keywords

  • Extracellular and receptor proteins
  • Laminin G domain
  • Tandem array

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Rupert Timpl

  • Dominic Tisi

  • Jan F. Talts

  • Zeynep Andac

  • Takako Sasaki

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free