This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1e4t

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1e4t.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1e4t.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1e4t| PDB=1e4t | SCENE= }}
{{STRUCTURE_1e4t| PDB=1e4t | SCENE= }}
-
'''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.
 +
-->
 +
{{ABSTRACT_PUBMED_11714914}}
==About this Structure==
==About this Structure==
-
1E4T 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].
+
1E4T 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==
==Reference==
Line 32: Line 36:
[[Category: Mouse]]
[[Category: Mouse]]
[[Category: Nmr structure]]
[[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 Tue Jul 1 00:09:01 2008''

Revision as of 21:09, 30 June 2008

Image:1e4t.png

Template:STRUCTURE 1e4t

SOLUTION STRUCTURE OF THE MOUSE DEFENSIN MBD-7

Template:ABSTRACT PUBMED 11714914

About this Structure

1E4T is a Single protein structure of sequence from Mus musculus. 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

Page seeded by OCA on Tue Jul 1 00:09:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e4t"
Personal tools