Sandbox Reserved 959
From Proteopedia
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==== Monomere structure ==== | ==== Monomere structure ==== | ||
| - | Each defensin monomer consists of three strands of antiparallel β-sheet incorporating 60% of the residues. Two β-turns and three disulfide bonds add further restrictions to the conformational freedom of the monomer.< | + | Each defensin monomer consists of three strands of antiparallel β-sheet incorporating 60% of the residues. Two β-turns and three disulfide bonds add further restrictions to the conformational freedom of the monomer.<ref>Gary Fujii, Michael E.Selsted, David Eisenberg. Defensins promote fusion and lysis of negatively charged membranes. Protein Science. 1993. Cambridge University.</ref> |
==== Dimere structure ==== | ==== Dimere structure ==== | ||
| - | The dimere is formed by joining identical β-strands of the two monomers together to create a symmetrical six-stranded P-sheet. This extended β-sheet twists and curls to form a basket-shaped structure that has a small slolvent-accessible channel passing through it. The base of the basket is hydrophobic while the top, which contains the N- and C-termini of the two defensin monomers, is polar. In the crystal structure, two dimers associate with one another by hydrophobic contact between the bases of each dimer basket. This dimer-of-dimers may be an essential feature of defensins’interaction with membranes.< | + | The dimere is formed by joining identical β-strands of the two monomers together to create a symmetrical six-stranded P-sheet. This extended β-sheet twists and curls to form a basket-shaped structure that has a small slolvent-accessible channel passing through it. The base of the basket is hydrophobic while the top, which contains the N- and C-termini of the two defensin monomers, is polar. In the crystal structure, two dimers associate with one another by hydrophobic contact between the bases of each dimer basket. This dimer-of-dimers may be an essential feature of defensins’interaction with membranes.<ref>Gary Fujii, Michael E.Selsted, David Eisenberg. Defensins promote fusion and lysis of negatively charged membranes. Protein Science. 1993. Cambridge University.</ref> |
=== Example === | === Example === | ||
Revision as of 18:27, 27 December 2014
| This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543. |
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Introduction
Defensins (DEF) are a family of proteins which are involved in host defense in the epithelia of mucosal surfaces such as those of the intestin, respiratory tract, urinary tract, and vagina. They are antimicrobial and cytotoxic. All the protein of the family are distinguished by a cystein motif and are encoded on the chromozome 8.[1]
There are many defensin but in this article we'll focus on the defensin-α-1. It is a polypeptide which is found in the microbicidal granules of neutrophils. It's syntetisize in the paneth cell, which plays a role in the defense process. defensin-α-1 plays a particular role in phagocite-mediated host defense. [2]
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