1bh1
From Proteopedia
(New page: 200px<br /><applet load="1bh1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bh1" /> '''STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 2...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1bh1.gif|left|200px]]<br /><applet load="1bh1" size=" | + | [[Image:1bh1.gif|left|200px]]<br /><applet load="1bh1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bh1" /> | caption="1bh1" /> | ||
'''STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 20 STRUCTURES'''<br /> | '''STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 20 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | D-Pro14 melittin was synthesized to investigate the effect of increasing | + | D-Pro14 melittin was synthesized to investigate the effect of increasing the angle of the bend in the hinge region between the helical segments of the molecule. Structural analysis by nuclear magnetic resonance indicated that, in methanol, the molecule consisted of two helices separated at Pro14, as in melittin. However, the two helices in D-Pro14 melittin were laterally displaced relative to each other by approximately 7 A, and in addition, there was a small rotation of the carboxyl-terminal helix relative to the amino-terminal helix around the long axis of the molecule. The peptide had less than 5% of the cytolytic activity of melittin. Modification of Arg22 with the 2,2,5,7,8-pentamethyl-chroman-6-sulphonyl (pmc) group restored hemolytic activity to close to that of unmodified melittin. Replacement of Arg22 with Phe was less effective in restoring hemolytic activity. Electron-paramagnetic resonance studies suggest that there is a positive correlation between hemolytic activity of the peptides and interaction with phospholipid bilayers. |
==About this Structure== | ==About this Structure== | ||
| - | 1BH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1BH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BH1 OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Apis mellifera]] | [[Category: Apis mellifera]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Barnham, K | + | [[Category: Barnham, K J.]] |
[[Category: Bartone, N.]] | [[Category: Bartone, N.]] | ||
[[Category: Curtain, C.]] | [[Category: Curtain, C.]] | ||
[[Category: Hewish, D.]] | [[Category: Hewish, D.]] | ||
[[Category: Kirkpatrick, A.]] | [[Category: Kirkpatrick, A.]] | ||
| - | [[Category: Liu, S | + | [[Category: Liu, S T.]] |
[[Category: Norton, R.]] | [[Category: Norton, R.]] | ||
[[Category: Rivett, D.]] | [[Category: Rivett, D.]] | ||
| Line 26: | Line 26: | ||
[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:10 2008'' |
Revision as of 09:55, 21 February 2008
|
STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 20 STRUCTURES
Overview
D-Pro14 melittin was synthesized to investigate the effect of increasing the angle of the bend in the hinge region between the helical segments of the molecule. Structural analysis by nuclear magnetic resonance indicated that, in methanol, the molecule consisted of two helices separated at Pro14, as in melittin. However, the two helices in D-Pro14 melittin were laterally displaced relative to each other by approximately 7 A, and in addition, there was a small rotation of the carboxyl-terminal helix relative to the amino-terminal helix around the long axis of the molecule. The peptide had less than 5% of the cytolytic activity of melittin. Modification of Arg22 with the 2,2,5,7,8-pentamethyl-chroman-6-sulphonyl (pmc) group restored hemolytic activity to close to that of unmodified melittin. Replacement of Arg22 with Phe was less effective in restoring hemolytic activity. Electron-paramagnetic resonance studies suggest that there is a positive correlation between hemolytic activity of the peptides and interaction with phospholipid bilayers.
About this Structure
1BH1 is a Single protein structure of sequence from Apis mellifera with as ligand. Full crystallographic information is available from OCA.
Reference
Structure and activity of D-Pro14 melittin., Hewish DR, Barnham KJ, Werkmeister JA, Kirkpatrick A, Bartone N, Liu ST, Norton RS, Curtain C, Rivetta DE, J Protein Chem. 2002 May;21(4):243-53. PMID:12168695
Page seeded by OCA on Thu Feb 21 11:55:10 2008
