1qfb: Difference between revisions

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[[Image:1qfb.jpg|left|200px]]
[[Image:1qfb.jpg|left|200px]]


{{Structure
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|LIGAND= <scene name='pdbligand=DTR:D-TRYPTOPHAN'>DTR</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>
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|DOMAIN=
{{STRUCTURE_1qfb| PDB=1qfb  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfb OCA], [http://www.ebi.ac.uk/pdbsum/1qfb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qfb RCSB]</span>
}}


'''THE CYCLIC PEPTIDE CONTRYPHAN-R FROM CONUS RADIATUS'''
'''THE CYCLIC PEPTIDE CONTRYPHAN-R FROM CONUS RADIATUS'''
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==About this Structure==
==About this Structure==
1QFB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFB OCA].  
1QFB is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFB OCA].  


==Reference==
==Reference==
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[[Category: Olivera, B M.]]
[[Category: Olivera, B M.]]
[[Category: Pallaghy, P K.]]
[[Category: Pallaghy, P K.]]
[[Category: conus peptide]]
[[Category: Conus peptide]]
[[Category: cyclic peptide]]
[[Category: Cyclic peptide]]
[[Category: d-configuration]]
[[Category: D-configuration]]
[[Category: disulfide bridge]]
[[Category: Disulfide bridge]]
[[Category: stiff-tail syndrome]]
[[Category: Stiff-tail syndrome]]
[[Category: venom duct peptide]]
[[Category: Venom duct peptide]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:42 2008''

Revision as of 03:11, 3 May 2008

File:1qfb.jpg

Template:STRUCTURE 1qfb

THE CYCLIC PEPTIDE CONTRYPHAN-R FROM CONUS RADIATUS


Overview

Contryphan-R is a disulfide-constrained octapeptide containing a D-tryptophan that was isolated recently from venom of the cone shell Conus radiatus. The polypeptide is present in two forms in solution due to cis-trans isomerization at hydroxyproline 3. The solution structure of the major form of this unusual polypeptide, determined from NMR data, consists of a well-defined fold containing a non-hydrogen-bonded chain reversal from Gly1 to Glu5, which includes a cis-hydroxyproline and a D-Trp, and a type I beta-turn from Glu5 to Cys8. The presence of a putative salt bridge between the Glu5 carboxyl group and the N-terminal ammonium group is investigated by using various solvation models during energy minimization and is compared with the results of a pH titration. A comparison of the structure of contryphan-R with other cyclic peptide structures highlights some of the key structural determinants of these peptides and suggests that the contryphan-R fold could be exploited as a scaffold onto which unrelated protein binding surfaces could be grafted. Comparison with small disulfide-bridged loops in larger proteins shows that contryphan-R is similar to a commonly occurring loop structure found in proteins.

About this Structure

1QFB is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Solution structure of contryphan-R, a naturally occurring disulfide-bridged octapeptide containing D-tryptophan: comparison with protein loops., Pallaghy PK, Melnikova AP, Jimenez EC, Olivera BM, Norton RS, Biochemistry. 1999 Aug 31;38(35):11553-9. PMID:10471307 Page seeded by OCA on Sat May 3 06:11:53 2008

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