1uva

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(New page: 200px<br /> <applet load="1uva" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uva, resolution 2.50&Aring;" /> '''LIPID BINDING IN RI...)
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Revision as of 18:09, 29 October 2007

Image:1uva.gif

1uva, resolution 2.50Å

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LIPID BINDING IN RICE NONSPECIFIC LIPID TRANSFER PROTEIN-1 COMPLEXES FROM ORYZA SATIVA

Overview

Nonspecific lipid transfer proteins (nsLTPs) facilitate the transfer of, phospholipids, glycolipids, fatty acids and steroids between membranes, with wide-ranging binding affinities. Three crystal structures of rice, nsLTP1 from Oryza sativa, complexed with myristic (MYR), palmitic (PAL) or, stearic acid (STE) were determined. The overall structures of the rice, nsLTP1 complexes belong to the four-helix bundle folding with a long, C-terminal loop. The nsLTP1-MYR and the nsLTP1-STE complexes bind a single, fatty acid while the nsLTP1-PAL complex binds two molecules of fatty, acids. The C-terminal loop region is elastic in order to accommodate a, diverse range of lipid molecules. The lipid molecules interact with the, nsLTP1-binding cavity mainly with hydrophobic interactions. Significant, ... [(full description)]

About this Structure

1UVA is a [Single protein] structure of sequence from [Oryza sativa] with MYR as [ligand]. Full crystallographic information is available from [OCA].

Reference

Lipid binding in rice nonspecific lipid transfer protein-1 complexes from Oryza sativa., Cheng HC, Cheng PT, Peng P, Lyu PC, Sun YJ, Protein Sci. 2004 Sep;13(9):2304-15. Epub 2004 Aug 4. PMID:15295114

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