1e4t
From Proteopedia
(New page: 200px<br /><applet load="1e4t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e4t" /> '''SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1e4t.jpg|left|200px]]<br /><applet load="1e4t" size=" | + | [[Image:1e4t.jpg|left|200px]]<br /><applet load="1e4t" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e4t" /> | caption="1e4t" /> | ||
'''SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD-7'''<br /> | '''SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD-7'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Defensins are cationic and cysteine-rich peptides that play a crucial role | + | Defensins are cationic and cysteine-rich peptides that play a crucial role in the host defense against microorganisms of many organisms by their capability to permeabilize bacterial membranes. The low sequence similarity among the members of the large mammalian beta-defensin family suggests that their antimicrobial activity is largely independent of their primary structure. To investigate to what extent these defensins share a similar fold, the structures of the two human beta-defensins, hBD-1 and hBD-2, as well as those of two novel murine defensins, termed mBD-7 and mBD-8, were determined by nuclear magnetic resonance spectroscopy. All four defensins investigated share a striking similarity on the level of secondary and tertiary structure including the lack of a distinct hydrophobic core, suggesting that the fold is mainly stabilized by the presence of three disulfide bonds. In addition to the overall shape of the molecules, the ratio of solvent-exposed polar and hydrophobic side chains is also very similar among the four defensins investigated. It is significant that beta-defensins do not exhibit a common pattern of charged and hydrophobic residues on the protein surface and that the beta-defensin-specific fold appears to accommodate a wide range of different amino acids at most sequence positions. In addition to the implications for the mode of biological defensin actions, these findings are of particular interest because beta-defensins have been suggested as lead compounds for the development of novel peptide antibiotics for the therapy of infectious diseases. |
==About this Structure== | ==About this Structure== | ||
| - | 1E4T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1E4T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E4T OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Adermann, K.]] | [[Category: Adermann, K.]] | ||
[[Category: Bauer, F.]] | [[Category: Bauer, F.]] | ||
| - | [[Category: Forssmann, W | + | [[Category: Forssmann, W G.]] |
[[Category: Kluver, E.]] | [[Category: Kluver, E.]] | ||
[[Category: Roesch, P.]] | [[Category: Roesch, P.]] | ||
| Line 24: | Line 24: | ||
[[Category: nmr structure]] | [[Category: nmr structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:48 2008'' |
Revision as of 10:23, 21 February 2008
|
SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD-7
Overview
Defensins are cationic and cysteine-rich peptides that play a crucial role in the host defense against microorganisms of many organisms by their capability to permeabilize bacterial membranes. The low sequence similarity among the members of the large mammalian beta-defensin family suggests that their antimicrobial activity is largely independent of their primary structure. To investigate to what extent these defensins share a similar fold, the structures of the two human beta-defensins, hBD-1 and hBD-2, as well as those of two novel murine defensins, termed mBD-7 and mBD-8, were determined by nuclear magnetic resonance spectroscopy. All four defensins investigated share a striking similarity on the level of secondary and tertiary structure including the lack of a distinct hydrophobic core, suggesting that the fold is mainly stabilized by the presence of three disulfide bonds. In addition to the overall shape of the molecules, the ratio of solvent-exposed polar and hydrophobic side chains is also very similar among the four defensins investigated. It is significant that beta-defensins do not exhibit a common pattern of charged and hydrophobic residues on the protein surface and that the beta-defensin-specific fold appears to accommodate a wide range of different amino acids at most sequence positions. In addition to the implications for the mode of biological defensin actions, these findings are of particular interest because beta-defensins have been suggested as lead compounds for the development of novel peptide antibiotics for the therapy of infectious diseases.
About this Structure
1E4T is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity., Bauer F, Schweimer K, Kluver E, Conejo-Garcia JR, Forssmann WG, Rosch P, Adermann K, Sticht H, Protein Sci. 2001 Dec;10(12):2470-9. PMID:11714914
Page seeded by OCA on Thu Feb 21 12:23:48 2008
