HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Papers In Press, published online ahead of print February 1, 2004
J. Lipid Res., doi:10.1194/jlr.M300113-JLR200

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: M300113-JLR200v1 45/2/232    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Reese, A. J. Articles by Banaszak, L. J. Search for Related Content PubMed PubMed Citation Articles by Reese, A. J. Articles by Banaszak, L. J. Social Bookmarking                      What's this?

Journal of Lipid Research, Vol. 45, 232-243, February 2004
Copyright © 2004 by American Society for Biochemistry and Molecular Biology

Specificity determinants for lipids bound to ß-barrel proteins

Amy J. Reese^* and Leonard J. Banaszak^1,

^* Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO
Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN

¹ To whom correspondence should be addressed. e-mail: banas001{at}umn.edu

The family of proteins accountable for the intracellular movement of lipids is characterized by a 10-stranded ß-barrel that forms an internalized cavity varying in size and binding preferences. The loop connecting ß-strands E and F (the fifth and sixth strands) is the most striking conformational difference between adipocyte lipid binding protein (ALBP; fatty acids) and cellular retinoic acid binding protein type I (CRABP I). A three-residue mutation was made in wild-type (WT)-ALBP [ALBP with a three-residue mutation (EF-ALBP)] to mimic CRABP I. Crystal structures of ligand-free and EF-ALBP with bound oleic acid were solved to resolutions of 1.5 Å and 1.7 Å, respectively, and compared with previous studies of WT-ALBP. The changes in three residues of one loop of the protein appear to have altered the positioning of the C₁₈ fatty acid, as observed in the electron density of EF-ALBP. The crystallographic studies made it possible to compare the protein conformation and ligand positioning with those found in the WT protein. Although the cavity binding sites in both the retinoid and fatty acid binding proteins are irregular, the ligand atoms appear to favor a relatively planar region of the cavities.

Preliminary chemical characterization of the mutant protein indicated changes in some binding properties and overall protein stability.

Abbreviations: ANS, 1-anilinonaphthalene-8-sulfonic acid; apo-, crystal structure without ligand bound; CRABP I, cellular retinoic acid binding protein type I; holo-, crystal structure with ligand bound; OA, oleic acid; PDB, Protein Data Bank; RA, retinoic acid; WT, wild-type

Supplementary key words adipocyte lipid binding protein • protein-ligand interaction • ligand binding • oleic acid • retinoic acid

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				D. H. Dyer, V. Wessely, K. T. Forest, and Q. Lan Three-dimensional structure/function analysis of SCP-2-like2 reveals differences among SCP-2 family members J. Lipid Res., March 1, 2008; 49(3): 644 - 653. [Abstract] [Full Text] [PDF]

				B. van den Berg, P. N. Black, W. M. Clemons Jr., and T. A. Rapoport Crystal Structure of the Long-Chain Fatty Acid Transporter FadL Science, June 4, 2004; 304(5676): 1506 - 1509. [Abstract] [Full Text] [PDF]