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3lyn

From Proteopedia

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[[Image:3lyn.jpg|left|200px]]
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{{STRUCTURE_3lyn| PDB=3lyn | SCENE= }}
{{STRUCTURE_3lyn| PDB=3lyn | SCENE= }}
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'''STRUCTURE OF GREEN ABALONE LYSIN DIMER'''
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===STRUCTURE OF GREEN ABALONE LYSIN DIMER===
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==Overview==
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Abalone sperm lysin is a 16 kDa acrosomal protein used by sperm to create a hole in the egg vitelline envelope. Lysins from seven California abalone exhibit species-specificity in binding to their egg receptor, and range in sequence identity from 63 % to 90 %. The crystal structure of the sperm lysin dimer from Haliotis fulgens (green abalone) has been determined to 1.71 A by multiple isomorphous replacement. Comparisons with the structure of the lysin dimer from Haliotis rufescens (red abalone) reveal a similar overall fold and conservation of features contributing to lysin's amphipathic character. The two structures do, however, exhibit differences in surface residues and electrostatics. A large clustering of non-conserved surface residues around the waist and clefts of the dimer, and differences in charged residues around these regions, indicate areas of the molecule which may be involved in species-specific egg recognition.
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(as it appears on PubMed at http://www.pubmed.gov), where 10698629 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10698629}}
==About this Structure==
==About this Structure==
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[[Category: Fertilization protein]]
[[Category: Fertilization protein]]
[[Category: Gamete recognition protein]]
[[Category: Gamete recognition protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:06:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 12:54:10 2008''

Revision as of 09:54, 3 July 2008

Template:STRUCTURE 3lyn

STRUCTURE OF GREEN ABALONE LYSIN DIMER

Template:ABSTRACT PUBMED 10698629

About this Structure

3LYN is a Single protein structure of sequence from Haliotis fulgens. Full crystallographic information is available from OCA.

Reference

The high resolution crystal structure of green abalone sperm lysin: implications for species-specific binding of the egg receptor., Kresge N, Vacquier VD, Stout CD, J Mol Biol. 2000 Mar 10;296(5):1225-34. PMID:10698629

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