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J. Biol. Chem., Vol. 266, Issue 34, 22899-22904, 12, 1991
K Garrison, AJ MacKrell and JH Fessler
Recent studies ascribed some biological actions of cell adhesion and cell
outgrowth to the carboxyl-most 1200 amino acids of vertebrate laminin A
chains. Here we report a 6.1-kilobase pair nucleotide cDNA sequence
encoding 1951 amino acids and the carboxyl end of a Drosophila laminin A
chain. It corresponds to the mouse laminin A domains G, I, II, and III, but
may represent a different type of laminin A chain. The arrangement of the
cysteine-rich repeats of domain III resembles that of B2 chains. However,
it has more amino acid identity with a portion of the mouse laminin A chain
domain IIIb than with other laminin repeats. Domains I and II are
consistent with an interrupted coiled- coil alpha-helical model of the long
arm of laminin but are poorly conserved. The G domain contains five
subdomains which are individually related to subdomains of vertebrate
laminin A chains. The results indicate that laminin G subdomains should be
considered individually, rather than merely as parts of a G-globule. A
sequence of hydroxyamino acids contributes to a spacer between two of the
subdomains. Stretches of hydroxyamino acids may be indicative of junctions
between domains of extracellular Drosophila proteins.
Drosophila laminin A chain sequence, interspecies comparison, and domain structure of a major carboxyl portion
Molecular Biology Institute, University of California, Los Angeles 90024-1570.
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