1hms

From Proteopedia
Revision as of 18:13, 12 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1hms" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hms, resolution 1.4Å" /> '''1.4 ANGSTROMS STRUCT...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search
File:1hms.gif


1hms, resolution 1.4Å

Drag the structure with the mouse to rotate

1.4 ANGSTROMS STRUCTURAL STUDIES ON HUMAN MUSCLE FATTY ACID BINDING PROTEIN: BINDING INTERACTIONS WITH THREE SATURATED AND UNSATURATED C18 FATTY ACIDS

OverviewOverview

BACKGROUND: Muscle fatty acid binding protein (M-FABP) is one of a family, of cytosolic lipid-binding proteins involved in fatty acid processing. In, order to investigate the precise interactions between M-FABP and its, ligands and to understand the structural basis of differential binding, affinity, we have compared the structures of M-FABP in complex with three, C18 fatty acids. RESULTS: We describe the crystal structures of M-FABP in, complex with n-octadecanoate (stearate), trans-delta 9-octadecenoate, (elaidate) and cis-delta 9-octadecenoate (oleate). These structures were, refined using least-squares positional and anisotropic temperature factor, refinement to final R-factors of 11.4%, 12.1% and 13.2% respectively for, all the data between 8.0 A and 1.4 A resolution. CONCLUSIONS: Stearate, elaidate and oleate each adopt highly similar U-shaped conformations when, they bind to M-FABP within a large interior binding cavity, which also, contains 13 ordered water molecules. The atomic structure of the protein, is virtually identical, regardless of the nature of the bound ligand. The, fatty acid is thought to enter the interior cavity of the protein via a, portal in its surface while interior solvent is released through a, secondary opening. The ligand affinity can be correlated with the, conformational energy and the solubility of the bound ligand.

About this StructureAbout this Structure

1HMS is a Single protein structure of sequence from Homo sapiens with OLA as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structural studies on human muscle fatty acid binding protein at 1.4 A resolution: binding interactions with three C18 fatty acids., Young AC, Scapin G, Kromminga A, Patel SB, Veerkamp JH, Sacchettini JC, Structure. 1994 Jun 15;2(6):523-34. PMID:7922029

Page seeded by OCA on Mon Nov 12 17:20:21 2007

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

OCA