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.


1fd4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fd4.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fd4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fd4| PDB=1fd4 | SCENE= }}
{{STRUCTURE_1fd4| PDB=1fd4 | SCENE= }}
-
'''HUMAN BETA-DEFENSIN 2'''
+
===HUMAN BETA-DEFENSIN 2===
-
==Overview==
+
<!--
-
Defensins are small cationic peptides that are crucial components of innate immunity, serving as both antimicrobial agents and chemoattractant molecules. The specific mechanism of antimicrobial activity involves permeabilization of bacterial membranes. It has been postulated that individual monomers oligomerize to form a pore through anionic membranes, although the evidence is only indirect. Here, we report two high resolution x-ray structures of human beta-defensin-2 (hBD2). The phases were experimentally determined by the multiwavelength anomalous diffraction method, utilizing a novel, rapid method of derivatization with halide ions. Although the shape and charge distribution of the monomer are similar to those of other defensins, an additional alpha-helical region makes this protein topologically distinct from the mammalian alpha- and beta-defensin structures reported previously. hBD2 forms dimers topologically distinct from that of human neutrophil peptide-3. The quaternary octameric arrangement of hBD2 is conserved in two crystal forms. These structures provide the first detailed description of dimerization of beta-defensins, and we postulate that the mode of dimerization of hBD2 is representative of other beta-defensins. The structural and electrostatic properties of the hBD2 octamer support an electrostatic charge-based mechanism of membrane permeabilization by beta-defensins, rather than a mechanism based on formation of bilayer-spanning pores.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10906336}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10906336 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10906336}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Defensin]]
[[Category: Defensin]]
[[Category: Human beta-defensin 2]]
[[Category: Human beta-defensin 2]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:11:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:04:26 2008''

Revision as of 00:04, 1 July 2008

Image:1fd4.png

Template:STRUCTURE 1fd4

HUMAN BETA-DEFENSIN 2

Template:ABSTRACT PUBMED 10906336

About this Structure

1FD4 is a Single protein structure. Full crystallographic information is available from OCA.

Reference

The structure of human beta-defensin-2 shows evidence of higher order oligomerization., Hoover DM, Rajashankar KR, Blumenthal R, Puri A, Oppenheim JJ, Chertov O, Lubkowski J, J Biol Chem. 2000 Oct 20;275(42):32911-8. PMID:10906336

Page seeded by OCA on Tue Jul 1 03:04:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fd4"
Personal tools