1e4t
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1e4t.jpg|left|200px]] | [[Image:1e4t.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1e4t", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1e4t| PDB=1e4t | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD-7''' | '''SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD-7''' | ||
| Line 32: | Line 29: | ||
[[Category: Schweimer, K.]] | [[Category: Schweimer, K.]] | ||
[[Category: Sticht, H.]] | [[Category: Sticht, H.]] | ||
| - | [[Category: | + | [[Category: Defensin]] |
| - | [[Category: | + | [[Category: Mouse]] |
| - | [[Category: | + | [[Category: Nmr structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:39:52 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 11:39, 2 May 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 Fri May 2 14:39:52 2008
