1qfb
From Proteopedia
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|PDB= 1qfb |SIZE=350|CAPTION= <scene name='initialview01'>1qfb</scene> | |PDB= 1qfb |SIZE=350|CAPTION= <scene name='initialview01'>1qfb</scene> | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |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> | ||
}} | }} | ||
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[[Category: Olivera, B M.]] | [[Category: Olivera, B M.]] | ||
[[Category: Pallaghy, P K.]] | [[Category: Pallaghy, P K.]] | ||
- | [[Category: NH2]] | ||
[[Category: conus peptide]] | [[Category: conus peptide]] | ||
[[Category: cyclic peptide]] | [[Category: cyclic peptide]] | ||
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[[Category: venom duct peptide]] | [[Category: venom duct peptide]] | ||
- | ''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 23:12:42 2008'' |
Revision as of 20:12, 30 March 2008
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Ligands: | , , | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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 of sequence from [1]. 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
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