1uvb: Difference between revisions

Line 4:

==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.

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==

Line 13:

[[Category: Oryza sativa]]

[[Category: Single protein]]

[[Category: Cheng, H.C.]]

[[Category: Cheng, H C.]]

[[Category: Cheng, P.T.]]

[[Category: Cheng, P T.]]

[[Category: Lyu, P.C.]]

[[Category: Lyu, P C.]]

[[Category: Peng, P.]]

[[Category: Sun, Y.J.]]

[[Category: Sun, Y J.]]

[[Category: PAM]]

[[Category: fatty acid binding]]

Line 25:

[[Category: rice]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun~~ Feb ~~3 10~~:08:19 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:41 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 13: / Line 13: @@
 [[Category: Oryza sativa]]
 [[Category: Single protein]]
-[[Category: Cheng, H.C.]]
+[[Category: Cheng, H C.]]
-[[Category: Cheng, P.T.]]
+[[Category: Cheng, P T.]]
-[[Category: Lyu, P.C.]]
+[[Category: Lyu, P C.]]
 [[Category: Peng, P.]]
-[[Category: Sun, Y.J.]]
+[[Category: Sun, Y J.]]
 [[Category: PAM]]
 [[Category: fatty acid binding]]
@@ Line 25: / Line 25: @@
 [[Category: rice]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:08:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:41 2008''