1e4t: Difference between revisions

Revision as of 00:09, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1e4t.png

Template:STRUCTURE 1e4t

SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD-7SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD-7

Template:ABSTRACT PUBMED 11714914

About this StructureAbout this Structure

1E4T is a Single protein structure of sequence from Mus musculus. Full experimental information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD-7'''
+===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.
+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}}
 ==About this Structure==
-E4T is a [[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].
+E4T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E4T OCA].
 ==Reference==
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