1d9j

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1d9j.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1d9j.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1d9j| PDB=1d9j | SCENE= }}
{{STRUCTURE_1d9j| PDB=1d9j | SCENE= }}
-
'''SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE'''
+
===SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE===
-
==Overview==
+
<!--
-
In order to elucidate the structure-antibiotic activity relationships of the peptides, the three-dimensional structures of two hybrid peptides, CA(1-8) - MA(1-12) and CA(1-8) - ME(1-12) in trifluoroethanol-containing aqueous solution were investigated by NMR spectroscopy. Both CA(1-8) - MA(1-12) and CA(1-8) - ME(1-12) have strong antibacterial activity but only CA(1-8) - ME(1-12) has hemolytic activity against human erythrocytes. CA(1-8) - MA(1-12) has a hydrophobic 310-helix of only two turns combined with one short helix in the N-terminus with a flexible hinge section in between. CA(1-8) - MA(1-12) has a severely bent structure in the middle of the peptide. These structural features as well as the low hydrophobicity of CA(1-8) - MA(1-12) seem to be crucial for the selective lysis against the membrane of prokaryotic cells. CA(1-8) - ME(1-12) has an alpha-helical structure of about three turns in the melittin domain and a flexible structure with one turn in the cecropin domain connected with a flexible hinge section in between, and these might be the structural features required for membrane disruption against prokaryotic and eukaryotic cells. The central hinge region (Gly9-Ile10-Gly11) in an amphipathic antibacterial peptide is considered to play an important role in providing the conformational flexibility required for ion channel formation of the C-terminal hydrophobic alpha-helix on cell membrane.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10424354}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10424354 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10424354}}
==About this Structure==
==About this Structure==
-
1D9J is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9J OCA].
+
1D9J is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9J OCA].
==Reference==
==Reference==
Line 24: Line 28:
[[Category: Oh, D.]]
[[Category: Oh, D.]]
[[Category: Helix-hinge-helix]]
[[Category: Helix-hinge-helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:36:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:42:37 2008''

Revision as of 19:42, 30 June 2008

Image:1d9j.png

Template:STRUCTURE 1d9j

SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE

Template:ABSTRACT PUBMED 10424354

About this Structure

1D9J is a Single protein structure. Full experimental information is available from OCA.

Reference

NMR structural characterization of cecropin A(1-8) - magainin 2(1-12) and cecropin A (1-8) - melittin (1-12) hybrid peptides., Oh D, Shin SY, Kang JH, Hahm KS, Kim KL, Kim Y, J Pept Res. 1999 May;53(5):578-89. PMID:10424354

Page seeded by OCA on Mon Jun 30 22:42:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1d9j"
Personal tools