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- W3148403045 abstract "Human lipoprotein[a] contains at least two high-molecular-weight, disulfide-linked apolipoproteins, apo[a] and apo B-100. Apo[a] is a highly glycosylated, hydrophilic apoprotein that somewhat resembles plasminogen by containing an extended kringle domain and a carboxyl-terminal serine protease domain. The apo[a] kringle domain is composed of 11 distinct kringle types. Ten of these display high sequence homology to plasminogen kringle 4 (PGK4). The crystallographic coordinates for PGK4 were used to generate three-dimensional molecular models of the apo[a] kringle types, and the lysine-binding region of PGK4 was used to compare the different potential receptor-ligand and ligand-binding sites contained in each different PGK4-like kringle of apo[a]. A receptor-ligand site can be proposed for each kringle type. Potential serine protease cleavage sites, containing arginine-threonine and threonine-arginine, are located on the surface of the kringles. The ligand-binding site of one apo[a] kringle model is almost ..." @default.
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- W3148403045 date "1993-01-01" @default.
- W3148403045 modified "2023-09-23" @default.
- W3148403045 title "Comparison of ligand-binding sites of modeled apo[a] kringle-like sequences in human lipoprotein[a]." @default.
- W3148403045 hasPublicationYear "1993" @default.
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