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.


1ews

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ews.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ews.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ews| PDB=1ews | SCENE= }}
{{STRUCTURE_1ews| PDB=1ews | SCENE= }}
-
'''THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1'''
+
===THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1===
-
==Overview==
+
<!--
-
NMR spectroscopy and simulated annealing calculations have been used to determine the three-dimensional structure of RK-1, an antimicrobial peptide from rabbit kidney recently discovered from homology screening based on the distinctive physicochemical properties of the corticostatins/defensins. RK-1 consists of 32 residues, including six cysteines arranged into three disulfide bonds. It exhibits antimicrobial activity against Escherichia coli and activates Ca(2+) channels in vitro. Through its physicochemical similarity, identical cysteine spacing, and linkage to the corticostatins/defensins, it was presumed to be a member of this family. However, RK-1 lacks both a large number of arginines in the primary sequence and a high overall positive charge, which are characteristic of this family of peptides. The three-dimensional solution structure, determined by NMR, consists of a triple-stranded antiparallel beta-sheet and a series of turns and is similar to the known structures of other alpha-defensins. This has enabled the definitive classification of RK-1 as a member of this family of antimicrobial peptides. Ultracentrifuge measurements confirmed that like rabbit neutrophil defensins, RK-1 is monomeric in solution, in contrast to human neutrophil defensins, which are dimeric.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11123900}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11123900 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11123900}}
==About this Structure==
==About this Structure==
-
1EWS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EWS OCA].
+
1EWS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EWS OCA].
==Reference==
==Reference==
Line 28: Line 32:
[[Category: Alpha defensin]]
[[Category: Alpha defensin]]
[[Category: Triple-stranded beta-sheet]]
[[Category: Triple-stranded beta-sheet]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:36:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:08:18 2008''

Revision as of 23:08, 30 June 2008

Template:STRUCTURE 1ews

THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1

Template:ABSTRACT PUBMED 11123900

About this Structure

1EWS is a Single protein structure of sequence from Oryctolagus cuniculus. Full experimental information is available from OCA.

Reference

Three-dimensional structure of RK-1: a novel alpha-defensin peptide., McManus AM, Dawson NF, Wade JD, Carrington LE, Winzor DJ, Craik DJ, Biochemistry. 2000 Dec 26;39(51):15757-64. PMID:11123900

Page seeded by OCA on Tue Jul 1 02:08:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools