Structure of chicken plasma retinol-binding protein.

Biochim Biophys Acta

Department of Organic Chemistry, University of Padua and Biopolymer Research Center, CNR, Padua, Italy.

Published: November 2001

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) A, b=53.56(6) A, c=73.41(8) A, 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.

Download full-text PDF

Source
http://dx.doi.org/10.1016/s0167-4838(01)00268-0DOI Listing

Publication Analysis

Top Keywords

chicken plasma
8
retinol-binding protein
8
structures mammalian
8
mammalian rbps
8
protein
5
structure
4
structure chicken
4
plasma retinol-binding
4
protein crystal
4
crystal structure
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!