Article
Disulfide bonding arrangements in active forms of the somatomedin B domain of human vitronectin.
Biochemistry - 1 Jun 2004
Kamikubo Yuichi, De Guzman Roberto, Kroon Gerard, Curriden Scott, Neels Jaap G, Churchill Michael J, Dawson Philip, Ołdziej Stanisław, Jagielska Anna, Scheraga Harold A, Loskutoff David J, Dyson H Jane
Abstract excerpt
The N-terminal cysteine-rich somatomedin B (SMB) domain (residues 1-44) of the human glycoprotein vitronectin contains the high-affinity binding sites for plasminogen activator inhibitor-1 (PAI-1) and the urokinase receptor (uPAR). We previously showed that the eight cysteine residues of recombinant SMB (rSMB) are organized into four disulfide bonds in a linear uncrossed pattern (Cys(5)-Cys(9), Cys(19)-Cys(21),...
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