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| [[Image:1e4s.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1e4s| PDB=1e4s | SCENE= }} | | {{STRUCTURE_1e4s| PDB=1e4s | SCENE= }} |
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| '''SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HBD-1'''
| | ===SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HBD-1=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11714914}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11714914 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11714914}} |
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| ==About this Structure== | | ==About this Structure== |
| 1E4S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E4S OCA]. | | 1E4S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E4S OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Human]] | | [[Category: Human]] |
| [[Category: Nmr structure]] | | [[Category: Nmr structure]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:39:45 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:08:54 2008'' |
