1a2d: Difference between revisions

Revision as of 12:40, 21 February 2008

PYRIDOXAMINE MODIFIED MURINE ADIPOCYTE LIPID BINDING PROTEIN

OverviewOverview

Adipocyte lipid-binding protein (ALBP) is a small (14.5 kDa) 10-stranded beta-barrel protein found in mammalian fat cells. The crystal structures of various holo-forms of ALBP have been solved and show the fatty acid ligand bound in a large (approximately 400 A3) cavity isolated from bulk solvent. Examination of the cavity suggests that it would be a good site for the creation of an artificial catalyst, as numerous well defined crystal structures of ALBP are available and past studies have shown the conformation to be reasonably tolerant to modification and mutagenesis. Previous work has shown ALBP to be a good protein scaffold for exploring enantio- and stereoselective reactions; two constructs, ALBP attached to either a pyridoxamine or a phenanthroline group at C117, have been chemically characterized. Both modified proteins have been crystallized and their structures solved and refined. The X-ray models have been used to examine the origin of the chiral selectivity seen in the products. It is apparent that these covalent adducts reduce the internal cavity volume, sterically limiting substrate interactions with the reactive groups, as well as solvent access to potential intermediates in the reaction pathway.

About this StructureAbout this Structure

1A2D is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structural characterization of two synthetic catalysts based on adipocyte lipid-binding protein., Ory JJ, Mazhary A, Kuang H, Davies RR, Distefano MD, Banaszak LJ, Protein Eng. 1998 Apr;11(4):253-61. PMID:9680187

Page seeded by OCA on Thu Feb 21 11:40:03 2008

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OCA

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-[[Image:1a2d.gif|left|200px]]<br /><applet load="1a2d" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1a2d, resolution 2.4&Aring;" />
 '''PYRIDOXAMINE MODIFIED MURINE ADIPOCYTE LIPID BINDING PROTEIN'''<br />
 ==Overview==
-Adipocyte lipid-binding protein (ALBP) is a small (14.5 kDa) 10-stranded, beta-barrel protein found in mammalian fat cells. The crystal structures, of various holo-forms of ALBP have been solved and show the fatty acid, ligand bound in a large (approximately 400 A3) cavity isolated from bulk, solvent. Examination of the cavity suggests that it would be a good site, for the creation of an artificial catalyst, as numerous well defined, crystal structures of ALBP are available and past studies have shown the, conformation to be reasonably tolerant to modification and mutagenesis., Previous work has shown ALBP to be a good protein scaffold for exploring, enantio- and stereoselective reactions; two constructs, ALBP attached to, either a pyridoxamine or a phenanthroline group at C117, have been, chemically characterized. Both modified proteins have been crystallized, and their structures solved and refined. The X-ray models have been used, to examine the origin of the chiral selectivity seen in the products. It, is apparent that these covalent adducts reduce the internal cavity volume, sterically limiting substrate interactions with the reactive groups, as, well as solvent access to potential intermediates in the reaction pathway.
+Adipocyte lipid-binding protein (ALBP) is a small (14.5 kDa) 10-stranded beta-barrel protein found in mammalian fat cells. The crystal structures of various holo-forms of ALBP have been solved and show the fatty acid ligand bound in a large (approximately 400 A3) cavity isolated from bulk solvent. Examination of the cavity suggests that it would be a good site for the creation of an artificial catalyst, as numerous well defined crystal structures of ALBP are available and past studies have shown the conformation to be reasonably tolerant to modification and mutagenesis. Previous work has shown ALBP to be a good protein scaffold for exploring enantio- and stereoselective reactions; two constructs, ALBP attached to either a pyridoxamine or a phenanthroline group at C117, have been chemically characterized. Both modified proteins have been crystallized and their structures solved and refined. The X-ray models have been used to examine the origin of the chiral selectivity seen in the products. It is apparent that these covalent adducts reduce the internal cavity volume, sterically limiting substrate interactions with the reactive groups, as well as solvent access to potential intermediates in the reaction pathway.
 ==About this Structure==
-A2D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A2D OCA].
+A2D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2D OCA].
 ==Reference==
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