1e4q

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[[Image:1e4q.gif|left|200px]]
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{{Seed}}
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[[Image:1e4q.png|left|200px]]
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{{STRUCTURE_1e4q| PDB=1e4q | SCENE= }}
{{STRUCTURE_1e4q| PDB=1e4q | SCENE= }}
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'''SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HBD-2'''
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===SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HBD-2===
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_11714914}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11714914 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11714914}}
==About this Structure==
==About this Structure==
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1E4Q 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=1E4Q OCA].
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1E4Q 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=1E4Q OCA].
==Reference==
==Reference==
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[[Category: Human]]
[[Category: Human]]
[[Category: Nmr structure]]
[[Category: Nmr structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:39:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:08:51 2008''

Revision as of 21:08, 30 June 2008

Image:1e4q.png

Template:STRUCTURE 1e4q

SOLUTION STRUCTURE OF THE HUMAN DEFENSIN HBD-2

Template:ABSTRACT PUBMED 11714914

About this Structure

1E4Q is a Single protein structure of sequence from Homo sapiens. Full experimental 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

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