2hzr
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2hzr.jpg|left|200px]] | [[Image:2hzr.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2hzr", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2hzr| PDB=2hzr | SCENE= }} | |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''Crystal structure of human apolipoprotein D (ApoD)''' | '''Crystal structure of human apolipoprotein D (ApoD)''' | ||
| Line 27: | Line 24: | ||
[[Category: Eichinger, A.]] | [[Category: Eichinger, A.]] | ||
[[Category: Skerra, A.]] | [[Category: Skerra, A.]] | ||
| - | [[Category: | + | [[Category: Beta barrel]] |
| - | [[Category: | + | [[Category: Bilin-binding protein]] |
| - | [[Category: | + | [[Category: Lipocalin]] |
| - | [[Category: | + | [[Category: Transport protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:54:32 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:54, 4 May 2008
Crystal structure of human apolipoprotein D (ApoD)
Overview
Human apolipoprotein D (ApoD) occurs in plasma associated with high density lipoprotein. Apart from the involvement in lipid metabolism, its binding activity for progesterone and arachidonic acid plays a role in cancer development and neurological diseases. The crystal structures of free ApoD and its complex with progesterone were determined at 1.8A resolution and reveal a lipocalin fold. The narrow, mainly uncharged pocket within the typical beta-barrel accommodates progesterone with its acetyl side chain oriented toward the bottom. The cavity adopts essentially the same shape in the absence of progesterone and allows complexation of arachidonic acid as another cognate ligand. Three of the four extended loops at the open end of the beta-barrel expose hydrophobic side chains, which is an unusual feature for lipocalins and probably effects association with the high density lipoprotein particle by mediating insertion into the lipid phase. This mechanism is in line with an unpaired Cys residue in the same surface region that can form a disulfide cross-link with apolipoprotein A-II.
About this Structure
2HZR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural insight into the dual ligand specificity and mode of high density lipoprotein association of apolipoprotein D., Eichinger A, Nasreen A, Kim HJ, Skerra A, J Biol Chem. 2007 Oct 19;282(42):31068-75. Epub 2007 Aug 14. PMID:17699160 Page seeded by OCA on Sun May 4 06:54:32 2008
