Laminin-type epidermal growth factor-like domai
SMART accession number:SM00180
Interpro abstract (IPR002049): Laminins [(PUBMED:2404817)] are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation. They are composed of distinct but related alpha, beta and gamma chains. The three chains form a cross-shaped molecule that consist of a long arm and three short globular arms. The long arm consist of a coiled coil structure contributed by all three chains and cross-linked by interchain disulphide bonds. Beside different types of globular domains each subunit contains, in its first half, consecutive repeats of about 60 amino acids in length that include eight conserved cysteines [(PUBMED:2666164)]. The tertiary structure [(PUBMED:8648630), (PUBMED:8648631)] of this domain is remotely similar in its N-terminal to that of the EGF-like module. It is known as a 'LE' or 'laminin-type EGF-like' domain. The number of copies of the LE domain in the different forms of laminins is highly variable; from 3 up to 22 copies have been found. A schematic representation of the topology of the four disulphide bonds in the LE domain is shown below.

+-|-----------+ | +--------+ +-----------------+
| | | | | | | |
'C': conserved cysteine involved in a disulphide bond
'a': conserved aromatic residue
'G': conserved glycine (lower case = less conserved)
's': region similar to the EGF-like domain
In mouse laminin gamma-1 chain, the seventh LE domain has been shown to be the only one that binds with a high affinity to nidogen [(PUBMED:7781764)]. The binding-sites are located on the surface within the loops C1-C3 and C5-C6 [(PUBMED:8648630), (PUBMED:8648631)]. Long consecutive arrays of LE domains in laminins form rod-like elements of limited flexibility [(PUBMED:2404817)], which determine the spacing in the formation of laminin networks of basement membranes [(PUBMED:8349613)].
Family alignment:
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There are 8870 EGF_Lam domains in 1681 proteins in SMART's nrdb database.

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