1qfb
From Proteopedia
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| - | [[Image:1qfb.jpg|left|200px]] | + | [[Image:1qfb.jpg|left|200px]] |
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| - | '''THE CYCLIC PEPTIDE CONTRYPHAN-R FROM CONUS RADIATUS''' | + | {{Structure |
| + | |PDB= 1qfb |SIZE=350|CAPTION= <scene name='initialview01'>1qfb</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE CYCLIC PEPTIDE CONTRYPHAN-R FROM CONUS RADIATUS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QFB is a [ | + | 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]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10471307 10471307] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Jimenez, E C.]] | [[Category: Jimenez, E C.]] | ||
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[[Category: venom duct peptide]] | [[Category: venom duct peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:36:36 2008'' |
Revision as of 11:36, 20 March 2008
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| 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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