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- W787025276 abstract " The method of isoraorphous replacement has been used to determine the crystal structure of human plasma prealbumin (Mwt. 56 000) Three derivatives were measured to a resolution of 2.5 A and a mercury derivative was re-measured with a long x-ray count time to improve the quality of the estimates of anomalous scatter. A protein Fourier synthesis has been calculated using phases determined from the anomalous and isomorphous differences. The conformation of the two polypeptide chains in the asymmetric unit of P2 1 2 1 2 (the crystal space group) has been determined. The chains in each monomer have an apparently identical conformation They are nearly fully extended and form an extensive network of (beta)-structure, Eight strands of (beta)-sheet in each monomer form a flattened cup shape the interior of which appears to be entirely hydrophobic. The ends and bottom of the cup are closed by loops in a random coil conformation. One loop contains a right-handed (alpha)-helix of about two turns. The top of the cup is closed by the second monomer,so that the front of this unit is a continuous 8-stranded (beta)-pleated sheet. The back of this is also formed by an 8-stranded p-sheet,but this is less regular. The dimers formed in this way interact so that their front sheets are opposed at a distance of 10 A. The thyroxine-binding site has been identified within the channel formed by the (beta)-sheets of opposed dimers. There are two possible binding sites, only one of which may be occupied in one molecule (on chemical evidence)." @default.
- W787025276 created "2016-06-24" @default.
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- W787025276 date "1973-01-01" @default.
- W787025276 modified "2023-09-26" @default.
- W787025276 title "Structural analysis of vitamin A transport system" @default.
- W787025276 hasPublicationYear "1973" @default.
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