2o8n

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{{STRUCTURE_2o8n| PDB=2o8n | SCENE= }}
{{STRUCTURE_2o8n| PDB=2o8n | SCENE= }}
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'''Crystal Structure of Mouse Apolipoprotein A-I Binding Protein'''
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===Crystal Structure of Mouse Apolipoprotein A-I Binding Protein===
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==Overview==
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The physiological changes that sperm undergo in the female reproductive tract rendering them fertilization-competent constitute the phenomenon of capacitation. Cholesterol efflux from the sperm surface and protein kinase A (PKA)-dependent phosphorylation play major regulatory roles in capacitation, but the link between these two phenomena is unknown. We report that apolipoprotein A-I binding protein (AI-BP) is phosphorylated downstream to PKA activation, localizes to both sperm head and tail domains, and is released from the sperm into the media during in vitro capacitation. AI-BP interacts with apolipoprotein A-I, the component of high-density lipoprotein involved in cholesterol transport. The crystal structure demonstrates that the subunit of the AI-BP homodimer has a Rossmann-like fold. The protein surface has a large two compartment cavity lined with conserved residues. This cavity is likely to constitute an active site, suggesting that AI-BP functions as an enzyme. The presence of AI-BP in sperm, its phosphorylation by PKA, and its release during capacitation suggest that AI-BP plays an important role in capacitation possibly providing a link between protein phosphorylation and cholesterol efflux.
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{{ABSTRACT_PUBMED_18202122}}
==About this Structure==
==About this Structure==
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[[Category: Protein binding]]
[[Category: Protein binding]]
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:26:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:37:30 2008''

Revision as of 18:37, 27 July 2008

Image:2o8n.png

Template:STRUCTURE 2o8n

Crystal Structure of Mouse Apolipoprotein A-I Binding Protein

Template:ABSTRACT PUBMED 18202122

About this Structure

2O8N is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Biochemical and structural characterization of apolipoprotein A-I binding protein, a novel phosphoprotein with a potential role in sperm capacitation., Jha KN, Shumilin IA, Digilio LC, Chertihin O, Zheng H, Schmitz G, Visconti PE, Flickinger CJ, Minor W, Herr JC, Endocrinology. 2008 May;149(5):2108-20. Epub 2008 Jan 17. PMID:18202122

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