1g7n: Difference between revisions

Revision as of 04:50, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1g7n.png

Template:STRUCTURE 1g7n

Toward changing specificity: adipocyte lipid binding protein mutant, apo formToward changing specificity: adipocyte lipid binding protein mutant, apo form

Template:ABSTRACT PUBMED 14594993

About this StructureAbout this Structure

1G7N is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Specificity determinants for lipids bound to beta-barrel proteins., Reese AJ, Banaszak LJ, J Lipid Res. 2004 Feb;45(2):232-43. Epub 2003 Nov 1. PMID:14594993

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Toward changing specificity: adipocyte lipid binding protein mutant, apo form'''
+===Toward changing specificity: adipocyte lipid binding protein mutant, apo form===
-==Overview==
+<!--
-The family of proteins accountable for the intracellular movement of lipids is characterized by a 10-stranded beta-barrel that forms an internalized cavity varying in size and binding preferences. The loop connecting beta-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 A and 1.7 A, 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14594993}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14594993 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14594993}}
 ==About this Structure==
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 [[Category: Fatty acid binding protein]]
 [[Category: Protein engineering]]
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