PROSITE documentation PDOC51117
Laminin N-terminal (LN) domain profile


Laminin is a large molecular weight glycoprotein present only in basement membranes in almost every animal tissue. Each laminin is a heterotrimer assembled from α, β and γ chain subunits, secreted and incorporated into cell-associated extracellular matrices [1].

Basement membrane assembly is a cooperative process in which laminins polymerize through their N-terminal domain (LN or domain VI) and anchor to the cell surface through their G domains (see <PDOC50025>). Netrins may also associate with this network through heterotypic LN domain interactions [2]. This leads to cell signaling through integrins and dystroglycan (and possibly other receptors) recruited to the adherent laminin. This LN domain dependent self-assembly is considered to be crucial for the integrity of basement membranes, as highlighted by genetic forms of muscular dystrophy containing the deletion of the LN module from the α 2 laminin chain [3].

The laminin N-terminal domain is found in all laminin and netrin subunits except laminin α 3A, α 4 and γ 2.

The profile we developed covers the whole laminin N-terminal domain.

Last update:

April 2005 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

LAMININ_NTER, PS51117; Laminin N-terminal domain profile  (MATRIX)


1AuthorsColognato H. Yurchenco P.D.
TitleForm and function: the laminin family of heterotrimers.
SourceDev. Dyn. 218:213-234(2000).
PubMed ID10842354

2AuthorsYurchenco P.D. Cheng Y.S.
TitleSelf-assembly and calcium-binding sites in laminin. A three-arm interaction model.
SourceJ. Biol. Chem. 268:17286-17299(1993).
PubMed ID8349613

3AuthorsXu H. Wu X.R. Wewer U.M. Engvall E.
TitleMurine muscular dystrophy caused by a mutation in the laminin alpha 2 (Lama2) gene.
SourceNat. Genet. 8:297-302(1994).
PubMed ID7874173

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