Sperm coating mechanism from the 1.8 A crystal structure of PDC-109-phosphorylcholine complex (Q27638765)

5

object named as

Juan J Calvete

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author name string

David A Wah

1

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Carlos Fernández-Tornero

2

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Antonio Romero

Purification and biochemical characterization of three major acidic proteins (BSP-A1, BSP-A2 and BSP-A3) from bovine seminal plasma

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publication date

April 2002

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published in

Structure

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volume

10

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issue

4

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page(s)

505-14

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cites work

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Primary structure of PDC-109, a major protein constituent of bovine seminal plasma

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The major protein of bull seminal plasma: biosynthesis and biological function

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The primary structure of BSP-30K, a major lipid-, gelatin-, and heparin-binding glycoprotein of bovine seminal plasma

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Complementary deoxyribonucleic acid cloning and tissue expression of BSP-A3 and BSP-30-kDa: phosphatidylcholine and heparin-binding proteins of bovine seminal plasma

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Major proteins of bovine seminal plasma modulate sperm capacitation by high-density lipoprotein

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Major proteins of bovine seminal vesicles bind to spermatozoa

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Phosphatidylcholine-binding proteins of bovine seminal plasma modulate capacitation of spermatozoa by heparin

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Major proteins of bovine seminal plasma and high-density lipoprotein induce cholesterol efflux from epididymal sperm

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Seminal plasma choline phospholipid-binding proteins stimulate cellular cholesterol and phospholipid efflux

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Characterization of lipid efflux particles generated by seminal phospholipid-binding proteins

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Cholesterol efflux-mediated signal transduction in mammalian sperm. beta-cyclodextrins initiate transmembrane signaling leading to an increase in protein tyrosine phosphorylation and capacitation

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Heparin and high-density lipoprotein mediate bovine sperm capacitation by different mechanisms

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Localization and structural characterization of an oligosaccharide O-linked to bovine PDC-109. Quantitation of the glycoprotein in seminal plasma and on the surface of ejaculated and capacitated spermatozoa

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The structure of the O-linked carbohydrate chain of bovine seminal plasma protein PDC-109 revised by 1 H-NMR spectroscopy A correction

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Characterisation of the conformational and quaternary structure-dependent heparin-binding region of bovine seminal plasma protein PDC-109

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Interaction of a novel class of phospholipid-binding proteins of bovine seminal fluid with different affinity matrices

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Type II domains of BSP-A1/-A2 proteins: binding properties, lipid efflux, and sperm capacitation potential

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Biophysical characterization of the interaction of bovine seminal plasma protein PDC-109 with phospholipid vesicles

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Biophysical study of the perturbation of model membrane structure caused by seminal plasma protein PDC-109.

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Conformational Features and Thermal Stability of Bovine Seminal Plasma Protein PDC-109 Oligomers and Phosphorylcholine-Bound Complexes

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Influence of the bovine seminal plasma protein PDC-109 on the physical state of membranes.

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Crystallization and preliminary X-ray diffraction analysis of bovine seminal plasma PDC-109, a protein composed of two fibronectin type II domains

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Refined solution structure and ligand-binding properties of PDC-109 domain b. A collagen-binding type II domain

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AMoRe: an automated package for molecular replacement

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Interface Characterization of the Type II Module Pair from Fibronectin†

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Role of seminal plasma phospholipid-binding proteins in sperm membrane lipid modification that occurs during capacitation

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Membrane insertion and lipid-protein interactions of bovine seminal plasma protein PDC-109 investigated by spin-label electron spin resonance spectroscopy

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A Procedure for the Large-Scale Isolation of Major Bovine Seminal Plasma Proteins

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