1h8p

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==Overview==
==Overview==
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Bovine seminal plasma PDC-109 binds to sperm surface choline lipids and, promotes sperm capacitation by stimulating the efflux of cholesterol and, phospholipids. The structure of PDC-109 with bound phosphorylcholine was, solved using MAD data of a single platinum site. Its two globular (40 x 50, x 20 A(3)) Fn2 domains are linked and clustered by a short polypeptide., The choline binding sites lie at the same face of the molecule., Phosphorylcholine binds to the Fn2 domains through a cation-pi interaction, between the quaternary ammonium group and a core tryptophan, plus hydrogen, bonding between hydroxyls of exposed tyrosines and the phosphate group., The structure of the PDC-109-oPC complex provides a structural ground for, the sperm membrane-coating mechanism underlying PDC-109-induced, capacitation.
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Bovine seminal plasma PDC-109 binds to sperm surface choline lipids and promotes sperm capacitation by stimulating the efflux of cholesterol and phospholipids. The structure of PDC-109 with bound phosphorylcholine was solved using MAD data of a single platinum site. Its two globular (40 x 50 x 20 A(3)) Fn2 domains are linked and clustered by a short polypeptide. The choline binding sites lie at the same face of the molecule. Phosphorylcholine binds to the Fn2 domains through a cation-pi interaction between the quaternary ammonium group and a core tryptophan, plus hydrogen bonding between hydroxyls of exposed tyrosines and the phosphate group. The structure of the PDC-109-oPC complex provides a structural ground for the sperm membrane-coating mechanism underlying PDC-109-induced capacitation.
==About this Structure==
==About this Structure==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Calvete, J.J.]]
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[[Category: Calvete, J J.]]
[[Category: Fernandez-Tornero, C.]]
[[Category: Fernandez-Tornero, C.]]
[[Category: Romero, A.]]
[[Category: Romero, A.]]
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[[Category: Wah, D.A.]]
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[[Category: Wah, D A.]]
[[Category: PC]]
[[Category: PC]]
[[Category: phosphorylcholine-binding protein]]
[[Category: phosphorylcholine-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:47:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:58:42 2008''

Revision as of 10:58, 21 February 2008


1h8p, resolution 1.82Å

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BULL SEMINAL PLASMA PDC-109 FIBRONECTIN TYPE II MODULE

Overview

Bovine seminal plasma PDC-109 binds to sperm surface choline lipids and promotes sperm capacitation by stimulating the efflux of cholesterol and phospholipids. The structure of PDC-109 with bound phosphorylcholine was solved using MAD data of a single platinum site. Its two globular (40 x 50 x 20 A(3)) Fn2 domains are linked and clustered by a short polypeptide. The choline binding sites lie at the same face of the molecule. Phosphorylcholine binds to the Fn2 domains through a cation-pi interaction between the quaternary ammonium group and a core tryptophan, plus hydrogen bonding between hydroxyls of exposed tyrosines and the phosphate group. The structure of the PDC-109-oPC complex provides a structural ground for the sperm membrane-coating mechanism underlying PDC-109-induced capacitation.

About this Structure

1H8P is a Single protein structure of sequence from Bos taurus with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Sperm coating mechanism from the 1.8 A crystal structure of PDC-109-phosphorylcholine complex., Wah DA, Fernandez-Tornero C, Sanz L, Romero A, Calvete JJ, Structure. 2002 Apr;10(4):505-14. PMID:11937055

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