2hzr
From Proteopedia
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| - | [[Image:2hzr.jpg|left|200px]] | + | [[Image:2hzr.jpg|left|200px]] |
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| - | '''Crystal structure of human apolipoprotein D (ApoD)''' | + | {{Structure |
| + | |PDB= 2hzr |SIZE=350|CAPTION= <scene name='initialview01'>2hzr</scene>, resolution 1.800Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= APOD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of human apolipoprotein D (ApoD)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2HZR is a [ | + | 2HZR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HZR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17699160 17699160] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:23:41 2008'' |
Revision as of 15:23, 20 March 2008
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| , resolution 1.800Å | |||||||
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| Gene: | APOD (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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