ISSN:
1573-4943
Schlagwort(e):
calcium-activated protease
;
cDNA and gene structure
;
molecular evolution
;
calcium binding
;
domain structure
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Chemie und Pharmazie
Notizen:
Abstract The amino acid sequences of two subunits (80K and 30K) of calcium-activated neutral protease (CANP) were examined to clarify the structure-function relationship of CANP. The 80K subunit is composed of four clear domains (I–IV from the N-terminus). Domain II is a cysteine proteinase domain homologous to cathepsins B, L, and H. Domain IV is a calcium binding domain with four consecutive EF-hand structures known as typical calcium-binding sites found in calmodulin. The 30K subunit also has a clear domain structure (two domains). The N-terminal domain, a Gly-rich hydrophobic domain, probably determines the location of CANP through association with cellular membrane. The C-terminal domain is a calmodulinlike calcium-binding domain highly homologous to IV in the 80K subunit. The protease activity ascribable to II is regulated by 2 moles of built-in “calmodulins,” though its precise regulation mechanism is unknown. These results are discussed together with the molecular evolution of CANP on the basis of the gene structures of the two subunits.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00248823
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