This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1qfb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1qfb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qfb" /> '''THE CYCLIC PEPTIDE CONTRYPHAN-R FROM CONUS R...)
Line 1: Line 1:
-
[[Image:1qfb.jpg|left|200px]]<br /><applet load="1qfb" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1qfb.jpg|left|200px]]<br /><applet load="1qfb" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qfb" />
caption="1qfb" />
'''THE CYCLIC PEPTIDE CONTRYPHAN-R FROM CONUS RADIATUS'''<br />
'''THE CYCLIC PEPTIDE CONTRYPHAN-R FROM CONUS RADIATUS'''<br />
==Overview==
==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.
+
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==
==About this Structure==
-
1QFB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QFB OCA].
+
1QFB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] 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=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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10471307 10471307]
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10471307 10471307]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Jimenez, E.C.]]
+
[[Category: Jimenez, E C.]]
-
[[Category: Melnikova, A.P.]]
+
[[Category: Melnikova, A P.]]
-
[[Category: Norton, R.S.]]
+
[[Category: Norton, R S.]]
-
[[Category: Olivera, B.M.]]
+
[[Category: Olivera, B M.]]
-
[[Category: Pallaghy, P.K.]]
+
[[Category: Pallaghy, P K.]]
[[Category: NH2]]
[[Category: NH2]]
[[Category: conus peptide]]
[[Category: conus peptide]]
Line 25: Line 25:
[[Category: venom duct peptide]]
[[Category: venom duct peptide]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:37:58 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:58 2008''

Revision as of 12:39, 21 February 2008


1qfb

Drag the structure with the mouse to rotate

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] with as ligand. 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 Thu Feb 21 14:38:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools