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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.

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: ALL Other sequence(s) detected in Swiss-Prot: NONE

• Domain architecture view of Swiss-Prot proteins matching PS51117 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS51117 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS51117 • Scan Swiss-Prot/TrEMBL entries against PS51117 • view ligand binding statistics

Matching PDB structures: 2Y38 3TBD 3ZYG 3ZYI ... [ALL]

1	Authors	Colognato H., Yurchenco P.D.
	Title	Form and function: the laminin family of heterotrimers.
	Source	Dev. Dyn. 218:213-234(2000).
	PubMed ID	10842354
	DOI	10.1002/(SICI)1097-0177(200006)218:2<213::AID-DVDY1>3.0.CO;2-R

2	Authors	Yurchenco P.D., Cheng Y.S.
	Title	Self-assembly and calcium-binding sites in laminin. A three-arm interaction model.
	Source	J. Biol. Chem. 268:17286-17299(1993).
	PubMed ID	8349613

3	Authors	Xu H., Wu X.R., Wewer U.M., Engvall E.
	Title	Murine muscular dystrophy caused by a mutation in the laminin alpha 2 (Lama2) gene.
	Source	Nat. Genet. 8:297-302(1994).
	PubMed ID	7874173
	DOI	10.1038/ng1194-297

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