2hzr

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{{STRUCTURE_2hzr| PDB=2hzr | SCENE= }}
{{STRUCTURE_2hzr| PDB=2hzr | SCENE= }}
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'''Crystal structure of human apolipoprotein D (ApoD)'''
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===Crystal structure of human apolipoprotein D (ApoD)===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_17699160}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 17699160 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17699160}}
==About this Structure==
==About this Structure==
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[[Category: Lipocalin]]
[[Category: Lipocalin]]
[[Category: Transport protein]]
[[Category: Transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:54:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:18:09 2008''

Revision as of 21:18, 28 July 2008

Image:2hzr.jpg

Template:STRUCTURE 2hzr

Crystal structure of human apolipoprotein D (ApoD)

Template:ABSTRACT PUBMED 17699160

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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