Effector sites in the three-dimensional structure of mammalian sperm beta-acrosin (Q27628384)

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J A Read

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R Jones

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R L Brady

Boar acrosin is a two-chain molecule. Isolation and primary structure of the light chain; homology with the pro-part of other serine proteinases

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publication date

15 November 2000

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published in

Structure

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volume

8

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issue

11

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page(s)

1179-88

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cites work

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Boar acrosin digestion of the porcine egg coat, zona pellucida, and rearrangement of the zona proteins.

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Matrix degrading properties of sperm serine proteinase, acrosin

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Acrosin Accelerates the Dispersal of Sperm Acrosomal Proteins during Acrosome Reaction

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Identification of a zona-binding protein from boar spermatozoa as proacrosin

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Acrosin shows zona and fucose binding, novel properties for a serine proteinase

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Inhibition of sperm-zona binding by suramin, a potential ‘lead’ compound for design of new anti-fertility agents

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The head shapes of some mammalian spermatozoa and their possible relationship to the shape of the penetration slit through the zona pellucida

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Why did the sperm cross the cumulus? To get to the oocyte. Functions of the sperm surface proteins PH-20 and fertilin in arriving at, and fusing with, the egg.

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The polysulphate binding domain of human proacrosin/acrosin is involved in both the enzyme activation and spermatozoa-zona pellucida interaction

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Biological implications of a 3 A structure of dimeric antithrombin

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Specificity of binding of zona pellucida glycoproteins to sperm proacrosin and related proteins

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Site-directed mutagenesis of rabbit proacrosin. Identification of residues involved in zona pellucida binding

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The 2.3 A crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator

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Structural basis for chemical inhibition of human blood coagulation factor Xa

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Further fractionation of the glycoprotein families of porcine zona pellucida by anion-exchange HPLC and some characterization of the separated fractions

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Site-directed mutagenesis of boar proacrosin reveals residues involved in binding of zona pellucida glycoproteins

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Characterization of the functional domains of boar acrosin involved in nonenzymatic binding to homologous zona pellucida glycoproteins

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Some effects of zona pellucida glycoproteins and sulfated polymers on the autoactivation of boar sperm proacrosin and activity of beta-acrosin

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Zona pellucida-binding and fucose-binding of boar sperm acrosin is not correlated with proteolytic activity

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