1ijv

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spinqualitylabelsall models 1ijv, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HUMAN BETA-DEFENSIN-1

Overview

Defensins are a class of small cationic peptides found in higher organisms, that serve as both antimicrobial and cell signaling molecules. The exact, mechanism of the antimicrobial activity of defensins is not known, but two, models have been postulated, one involving pore formation and the other, involving nonspecific electrostatic interaction with the bacterial, membrane. Here we report the high resolution structures of human, beta-defensin-1 (hBD1) in two crystallographic space groups. The structure, of a single molecule is very similar to that of human beta-defensin-2, (hBD2), confirming the presence of an N-terminal alpha-helix. However, while the packing of hBD1 is conserved across both space groups, there is, no evidence for any larger quaternary structure similar to octameric hBD2., Furthermore, the topology of hBD1 dimers that are formed between monomers, in the asymmetric unit is distinct from both hBD2 and other mammalian, alpha-defensins. The structures of hBD1 and hBD2 provide a first step, toward understanding the structural basis of antimicrobial and chemotactic, properties of human beta-defensins.

About this Structure

1IJV is a Single protein structure of sequence from [1] with SO4, BR and K as ligands. Full crystallographic information is available from OCA.

Reference

The structure of human beta-defensin-1: new insights into structural properties of beta-defensins., Hoover DM, Chertov O, Lubkowski J, J Biol Chem. 2001 Oct 19;276(42):39021-6. Epub 2001 Aug 2. PMID:11486002

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