1bh1: Difference between revisions
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|PDB= 1bh1 |SIZE=350|CAPTION= <scene name='initialview01'>1bh1</scene> | |PDB= 1bh1 |SIZE=350|CAPTION= <scene name='initialview01'>1bh1</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | |LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh1 OCA], [http://www.ebi.ac.uk/pdbsum/1bh1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bh1 RCSB]</span> | |||
}} | }} | ||
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[[Category: Rivett, D.]] | [[Category: Rivett, D.]] | ||
[[Category: Werkmeister, J.]] | [[Category: Werkmeister, J.]] | ||
[[Category: hemolytic polypeptide]] | [[Category: hemolytic polypeptide]] | ||
[[Category: toxin]] | [[Category: toxin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:00:45 2008'' | ||
Revision as of 16:00, 30 March 2008
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| 1bh1 | |||||||||||||
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| Ligands: | NH2 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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
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