期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
卷 1550, 期 1, 页码 64-69出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0167-4838(01)00268-0
关键词
retinol-binding protein; retinoid; vitamin A; transthyretin
The crystal structure of the specific carrier of retinol (retinol-binding protein, RBP) purified from chicken plasma has been determined (space group P2(1)2(1)2(1), with a = 46.06(5) Angstrom, b = 53.56(6) Angstrom, c = 73.41(8) Angstrom, and one protein molecule in the asymmetric unit). Despite being obtained from a species phylogenetically distant from mammals, chicken holoRBP has an overall structure that closely resembles the previously determined structures of mammalian holoRBPs. The lack in chicken RBP of eight carboxy-terminal amino acid residues characteristic of mammalian RBPs does not significantly affect the protein structure. A distinctive feature of the avian protein is a better definition of the loop 63-67, close to the opening of the beta -barrel cavity accommodating the retinol molecule, which is rather disordered in the structures of mammalian RBPs. (C) 2001 Elsevier Science B.V. All rights reserved.
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