|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 .
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 .
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 .
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.
April 2005 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|LAMININ_NTER, PS51117; Laminin N-terminal domain profile (MATRIX)
|Sequences known to belong to this class detected by the profile:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
2Y38 3TBD 3ZYG 3ZYI ... [ALL]
||Yurchenco P.D., Cheng Y.S.
||Self-assembly and calcium-binding sites in laminin. A three-arm interaction model.
||J. Biol. Chem. 268:17286-17299(1993).
||Xu H., Wu X.R., Wewer U.M., Engvall E.
||Murine muscular dystrophy caused by a mutation in the laminin alpha 2 (Lama2) gene.
||Nat. Genet. 8:297-302(1994).
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