Human laminin B2 chain
The complete amino acid sequence of the human laminin B2 chains has been determined by sequencing of cDNA clones. The six overlapping clones studied cover approximately 7.5 kilobases of which 5312 nucleotides were sequenced from the 5' end. The open reading frame codes for a 33-residue signal peptide and a 1576-residue B2 chain proper, which is 189 residues less than in the highly homologous B1 chain. Computer analysis revealed that the B2 chain consists of distinct domains that contain helical structures, cysteine-rich repeats, and globular regions, as does the B1 chain. However, domain ..cap alpha.. and domain ..beta.. of the B1 chain have no counterpart in B2, and the number of cysteine-rich repeats is 12, or 1 less than in the B1 chain. The degree of homology between the two chains is highest in the cysteine repeat-containing domains III and V where 40% of the residues match. However, in helical domains I/II only 16% of residues match. The results demonstrate that the B1 and B2 chains of laminin are highly homologous proteins that are probably the products of related genes.
- Research Organization:
- Univ. of Oulu (Finland)
- OSTI ID:
- 6838322
- Journal Information:
- J. Biol. Chem.; (United States), Vol. 263:14
- Country of Publication:
- United States
- Language:
- English
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RECOMBINANT DNA
DNA SEQUENCING
SCLEROPROTEINS
AMINO ACID SEQUENCE
MOLECULAR STRUCTURE
ATP
MAN
PHOSPHORUS 32
SULFUR 35
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
DAYS LIVING RADIOISOTOPES
DNA
EVEN-ODD NUCLEI
ISOTOPES
LIGHT NUCLEI
MAMMALS
NUCLEI
NUCLEIC ACIDS
NUCLEOTIDES
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
PHOSPHORUS ISOTOPES
PRIMATES
PROTEINS
RADIOISOTOPES
STRUCTURAL CHEMICAL ANALYSIS
SULFUR ISOTOPES
VERTEBRATES
550201* - Biochemistry- Tracer Techniques