InterPro : IPR002049

Name  EGF-like, laminin Short Name  EGF_laminin
Type  Domain Description  Laminins []are the major noncollagenous components of basement membranesthat mediate cell adhesion, growth migration, and differentiation. They arecomposed of distinct but related alpha, beta and gamma chains. The threechains form a cross-shaped molecule that consist of a long arm and three shortglobular arms. The long arm consist of a coiled coil structure contributed byall three chains and cross-linked by interchain disulphide bonds.Beside different types of globular domains each subunit contains, in its firsthalf, consecutive repeats of about 60 amino acids in length that include eightconserved cysteines []. The tertiary structure [, ]of this domain isremotely similar in its N-terminal to that of the EGF-like module (see ). It is known as a 'LE' or 'laminin-type EGF-like' domain. Thenumber of copies of the LE domain in the different forms of laminins is highlyvariable; from 3 up to 22 copies have been found.A schematic representation of the topology of the four disulphide bonds inthe LE domain is shown below.+-------------------++-|-----------+ | +--------+ +-----------------+| | | | | | | |xxCxCxxxxxxxxxxxCxxxxxxxCxxCxxxxxGxxCxxCxxgaagxxxxxxxxxxxCxxsssssssssssssssssssssssssssssssssss'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 domainIn mouse laminin gamma-1 chain, the seventh LE domain has been shown to be theonly one that binds with a high affinity to nidogen []. The binding-sites arelocated on the surface within the loops C1-C3 and C5-C6 [, ]. Longconsecutive arrays of LE domains in laminins form rod-like elements of limitedflexibility [], which determine the spacing in the formation of lamininnetworks of basement membranes [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

2 Contains

Id Name Short Name Type
IPR013032 EGF-like, conserved site EGF-like_CS Conserved_site
IPR000742 Epidermal growth factor-like domain EG-like_dom Domain

0 Found In

0 Parent Features

6 Publications

First Author Title Year Journal Volume Pages
Beck K Structure and function of laminin: anatomy of a multidomain glycoprotein. 1990 FASEB J 4 148-60
Engel J EGF-like domains in extracellular matrix proteins: localized signals for growth and differentiation? 1989 FEBS Lett 251 1-7
Mayer U Low nidogen affinity of laminin-5 can be attributed to two serine residues in EGF-like motif gamma 2III4. 1995 FEBS Lett 365 129-32
Yurchenco PD Self-assembly and calcium-binding sites in laminin. A three-arm interaction model. 1993 J Biol Chem 268 17286-99
Stetefeld J Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site. 1996 J Mol Biol 257 644-57
Baumgartner R Structure of the nidogen binding LE module of the laminin gamma1 chain in solution. 1996 J Mol Biol 257 658-68



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)