v5.1.0.3
Cicer data from the Legume Information System
Type | Domain |
Description | This entry represents the laminin-type EGF-like domain (LE) found in Laminin subunit gamma-1 and Netrin-1 from Homo sapiens and Mus musculus. Laminins 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 that form a cross-shaped molecule consisting of a long arm and three short globular arms. The long arm has a coiled coil structure contributed by all three chains and cross-linked by interchain disulphide bonds [, ]. Beside the 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 []. The tertiary structure of this domain is remotely similar in its N-terminal to that of the EGF-like module [, ] (see ). 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.+-------------------+ +-|-----------+ | +--------+ +-----------------+| | | | | | | | 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 domain Long consecutive arrays of LE domains in laminins form rod-like elements of limited flexibility [ ], which determine the spacing in the formation of laminin networks of basement membranes [].Netrins control guidance of the central nervous system commissural axons and peripheral motor axons [ , , , ]. This protein also serves as a survival factor via its association with its receptors which prevent the initiation of apoptosis, thus being involved in tumorigenesis [, ]. |
Short Name | LE_dom |