1oiz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1oiz.jpg|left|200px]]
[[Image:1oiz.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1oiz |SIZE=350|CAPTION= <scene name='initialview01'>1oiz</scene>, resolution 1.88&Aring;
+
The line below this paragraph, containing "STRUCTURE_1oiz", creates the "Structure Box" on the page.
-
|SITE= <scene name='pdbsite=AC1:Trt+Binding+Site+For+Chain+A'>AC1</scene>
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=TRT:FRAGMENT+OF+TRITON+X-100'>TRT</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1oiz| PDB=1oiz | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oiz OCA], [http://www.ebi.ac.uk/pdbsum/1oiz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oiz RCSB]</span>
+
-
}}
+
'''THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN'''
'''THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN'''
Line 30: Line 27:
[[Category: Stocker, A.]]
[[Category: Stocker, A.]]
[[Category: Tomizaki, T.]]
[[Category: Tomizaki, T.]]
-
[[Category: ataxia]]
+
[[Category: Ataxia]]
-
[[Category: aved]]
+
[[Category: Aved]]
-
[[Category: tocopherol]]
+
[[Category: Tocopherol]]
-
[[Category: transfer protein]]
+
[[Category: Transfer protein]]
-
[[Category: transport]]
+
[[Category: Transport]]
-
[[Category: vitamin e]]
+
[[Category: Vitamin e]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:54:40 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:46:01 2008''
+

Revision as of 00:54, 3 May 2008

Image:1oiz.jpg

Template:STRUCTURE 1oiz

THE MOLECULAR BASIS OF VITAMIN E RETENTION: STRUCTURE OF HUMAN ALPHA-TOCOPHEROL TRANSFER PROTEIN


Overview

Alpha-tocopherol transfer protein (alpha-TTP) is a liver protein responsible for the selective retention of alpha-tocopherol from dietary vitamin E, which is a mixture of alpha, beta, gamma, and delta-tocopherols and the corresponding tocotrienols. The alpha-TTP-mediated transfer of alpha-tocopherol into nascent VLDL is the major determinant of plasma alpha-tocopherol levels in humans. Mutations in the alpha-TTP gene have been detected in patients suffering from low plasma alpha-tocopherol and ataxia with isolated vitamin E deficiency (AVED). The crystal structure of alpha-TTP reveals two conformations. In its closed tocopherol-charged form, a mobile helical surface segment seals the hydrophobic binding pocket. In the presence of detergents, an open conformation is observed, which probably represents the membrane-bound form. The selectivity of alpha-TTP for RRR-alpha-tocopherol is explained from the van der Waals contacts occurring in the lipid-binding pocket. Mapping the known mutations leading to AVED onto the crystal structure shows that no mutations occur directly in the binding pocket.

About this Structure

1OIZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The molecular basis of vitamin E retention: structure of human alpha-tocopherol transfer protein., Meier R, Tomizaki T, Schulze-Briese C, Baumann U, Stocker A, J Mol Biol. 2003 Aug 15;331(3):725-34. PMID:12899840 Page seeded by OCA on Sat May 3 03:54:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oiz"
Personal tools