1uva

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 5: Line 5:
==Overview==
==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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?15295114 (full description)]]
+
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, conformational changes were observed in the binding cavity and the, C-terminal loop of the rice nsLTP1 upon lipid binding.
==About this Structure==
==About this Structure==
-
1UVA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa]] with MYR as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UVA OCA]].
+
1UVA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa] with MYR as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UVA OCA].
==Reference==
==Reference==
Line 26: Line 26:
[[Category: rice]]
[[Category: rice]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:12:15 2007''
+
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:30:07 2007''

Revision as of 12:24, 5 November 2007


1uva, resolution 2.50Å

Drag the structure with the mouse to rotate

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, conformational changes were observed in the binding cavity and the, C-terminal loop of the rice nsLTP1 upon lipid binding.

About this Structure

1UVA is a Single protein structure of sequence from Oryza sativa with MYR as ligand. Structure known Active Site: AC1. 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

Page seeded by OCA on Mon Nov 5 14:30:07 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools