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.


2nls

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2nls.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2nls.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2nls| PDB=2nls | SCENE= }}
{{STRUCTURE_2nls| PDB=2nls | SCENE= }}
-
'''Human beta-defensin-1 (Mutant Gln24Ala)'''
+
===Human beta-defensin-1 (Mutant Gln24Ala)===
-
==Overview==
+
<!--
-
Defensins are small (30-45 amino acid residues) cationic proteins with broad antimicrobial activity against many bacteria and fungi, some enveloped viruses, and other activities such as chemoattraction of a range of different cell types to the sites of inflammation. These proteins represent attractive targets for developing novel antimicrobial agents and modulators of immune responses with therapeutic applicability. In this report, we present the results of functional and structural studies of 26 single-site mutants of human beta-defensin 1 (hBD1). All mutants were assayed for antimicrobial activity against Escherichia coli (ATCC strain 25922) and for chemotactic activity with CCR6-transfected HEK293 cells. To analyze the structural implications of mutagenesis and to verify the correctness of the disulfide connectivity, we used x-ray crystallography to conduct complete structural studies for 10 mutants in which the topology of disulfides was the same as in the native hBD1. Mutations did not induce significant changes of the tertiary structure, suggesting that the observed alterations of biological properties of the mutants were solely associated with changes in the respective side chains. We found that cationic residues located near the C terminus (Arg(29), Lys(31), Lys(33), and Lys(36)) of hBD1 define most of the anti-E. coli in vitro activity of this protein. In turn, nearly all mutations altering the CCR6-mediated chemotaxis are located at one area of the protein, defined by the N-terminal alpha-helical region (Asp(1)... Ser(8)) and a few topologically adjacent residues (Lys(22), Arg(29), and Lys(33)). These experimental results allow for the first time drafting of the CCR6-epitope for a defensin molecule.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17071614}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17071614 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17071614}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Defensin]]
[[Category: Defensin]]
[[Category: Mutant]]
[[Category: Mutant]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:37:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:38:53 2008''

Revision as of 05:39, 28 July 2008

Image:2nls.png

Template:STRUCTURE 2nls

Human beta-defensin-1 (Mutant Gln24Ala)

Template:ABSTRACT PUBMED 17071614

About this Structure

2NLS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Studies of the biological properties of human beta-defensin 1., Pazgier M, Prahl A, Hoover DM, Lubkowski J, J Biol Chem. 2007 Jan 19;282(3):1819-29. Epub 2006 Oct 27. PMID:17071614

Page seeded by OCA on Mon Jul 28 08:38:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nls"
Personal tools