1xkm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xkm.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xkm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xkm| PDB=1xkm | SCENE= }}
{{STRUCTURE_1xkm| PDB=1xkm | SCENE= }}
-
'''NMR structure of antimicrobial peptide distinctin in water'''
+
===NMR structure of antimicrobial peptide distinctin in water===
-
==Overview==
+
<!--
-
Many bioactive peptides, presenting an unstructured conformation in aqueous solution, are made resistant to degradation by posttranslational modifications. Here, we describe how molecular oligomerization in aqueous solution can generate a still unknown transport form for amphipathic peptides, which is more compact and resistant to proteases than forms related to any possible monomer. This phenomenon emerged from 3D structure, function, and degradation properties of distinctin, a heterodimeric antimicrobial compound consisting of two peptide chains linked by a disulfide bond. After homodimerization in water, this peptide exhibited a fold consisting of a symmetrical full-parallel four-helix bundle, with a well secluded hydrophobic core and exposed basic residues. This fold significantly stabilizes distinctin against proteases compared with other linear amphipathic peptides, without affecting its antimicrobial, hemolytic, and ion-channel formation properties after membrane interaction. This full-parallel helical orientation represents a perfect compromise between formation of a stable structure in water and requirement of a drastic structural rearrangement in membranes to elicit antimicrobial potential. Thus, distinctin can be claimed as a prototype of a previously unrecognized class of antimicrobial derivatives. These results suggest a critical revision of the role of peptide oligomerization whenever solubility or resistance to proteases is known to affect biological properties.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15840728}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15840728 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15840728}}
==About this Structure==
==About this Structure==
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKM OCA].
+
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKM OCA].
==Reference==
==Reference==
A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin., Raimondo D, Andreotti G, Saint N, Amodeo P, Renzone G, Sanseverino M, Zocchi I, Molle G, Motta A, Scaloni A, Proc Natl Acad Sci U S A. 2005 May 3;102(18):6309-14. Epub 2005 Apr 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15840728 15840728]
A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin., Raimondo D, Andreotti G, Saint N, Amodeo P, Renzone G, Sanseverino M, Zocchi I, Molle G, Motta A, Scaloni A, Proc Natl Acad Sci U S A. 2005 May 3;102(18):6309-14. Epub 2005 Apr 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15840728 15840728]
 +
 +
A novel heterodimeric antimicrobial peptide from the tree-frog Phyllomedusa distincta., Batista CV, Scaloni A, Rigden DJ, Silva LR, Rodrigues Romero A, Dukor R, Sebben A, Talamo F, Bloch C, FEBS Lett. 2001 Apr 6;494(1-2):85-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11297740 11297740]
[[Category: Amodeo, P.]]
[[Category: Amodeo, P.]]
[[Category: Andreotti, G.]]
[[Category: Andreotti, G.]]
Line 31: Line 37:
[[Category: Nmr structure]]
[[Category: Nmr structure]]
[[Category: Pore-forming peptide]]
[[Category: Pore-forming peptide]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:09:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:38:22 2008''

Revision as of 23:38, 28 July 2008

Image:1xkm.png

Template:STRUCTURE 1xkm

NMR structure of antimicrobial peptide distinctin in water

Template:ABSTRACT PUBMED 15840728

About this Structure

Full experimental information is available from OCA.

Reference

A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin., Raimondo D, Andreotti G, Saint N, Amodeo P, Renzone G, Sanseverino M, Zocchi I, Molle G, Motta A, Scaloni A, Proc Natl Acad Sci U S A. 2005 May 3;102(18):6309-14. Epub 2005 Apr 19. PMID:15840728

A novel heterodimeric antimicrobial peptide from the tree-frog Phyllomedusa distincta., Batista CV, Scaloni A, Rigden DJ, Silva LR, Rodrigues Romero A, Dukor R, Sebben A, Talamo F, Bloch C, FEBS Lett. 2001 Apr 6;494(1-2):85-9. PMID:11297740

Page seeded by OCA on Tue Jul 29 02:38:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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