1vrz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1vrz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vrz, resolution 1.05&Aring;" /> '''Helix turn helix mot...)
Line 1: Line 1:
-
[[Image:1vrz.gif|left|200px]]<br /><applet load="1vrz" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1vrz.gif|left|200px]]<br /><applet load="1vrz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1vrz, resolution 1.05&Aring;" />
caption="1vrz, resolution 1.05&Aring;" />
'''Helix turn helix motif'''<br />
'''Helix turn helix motif'''<br />
==Overview==
==Overview==
-
De novo design of supersecondary structures is expected to provide useful, molecular frameworks for the incorporation of functional sites as in, proteins. A 21 residue long, dehydrophenylalanine-containing peptide has, been de novo designed and its crystal structure determined. The apolar, peptide folds into a helical hairpin supersecondary structure with two, right-handed helices, connected by a tetraglycine linker. The helices of, the hairpin interact with each other through a combination of C-H.O and, N-H.O hydrogen bonds. The folding of the apolar peptide has been realized, without the help of either metal ions or disulphide bonds. A remarkable, feature of the peptide is the unanticipated occurrence of an anion binding, motif in the linker region, strikingly similar in conformation and, function to the "nest" motif seen in several proteins. The observation, supports the view for the possible emergence of rudimentary functions over, short sequence stretches in the early peptides under prebiotic conditions.
+
De novo design of supersecondary structures is expected to provide useful molecular frameworks for the incorporation of functional sites as in proteins. A 21 residue long, dehydrophenylalanine-containing peptide has been de novo designed and its crystal structure determined. The apolar peptide folds into a helical hairpin supersecondary structure with two right-handed helices, connected by a tetraglycine linker. The helices of the hairpin interact with each other through a combination of C-H.O and N-H.O hydrogen bonds. The folding of the apolar peptide has been realized without the help of either metal ions or disulphide bonds. A remarkable feature of the peptide is the unanticipated occurrence of an anion binding motif in the linker region, strikingly similar in conformation and function to the "nest" motif seen in several proteins. The observation supports the view for the possible emergence of rudimentary functions over short sequence stretches in the early peptides under prebiotic conditions.
==About this Structure==
==About this Structure==
-
1VRZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with ACT, ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1Q4F. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VRZ OCA].
+
1VRZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1Q4F. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRZ OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Inai, Y.]]
[[Category: Inai, Y.]]
-
[[Category: Ramagopal, U.A.]]
+
[[Category: Ramagopal, U A.]]
[[Category: Ramakumar, S.]]
[[Category: Ramakumar, S.]]
[[Category: Rudresh]]
[[Category: Rudresh]]
Line 23: Line 23:
[[Category: hth]]
[[Category: hth]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:08:26 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:38:00 2008''

Revision as of 13:38, 21 February 2008

Image:1vrz.gif

1vrz, resolution 1.05Å

Drag the structure with the mouse to rotate

Helix turn helix motif

Overview

De novo design of supersecondary structures is expected to provide useful molecular frameworks for the incorporation of functional sites as in proteins. A 21 residue long, dehydrophenylalanine-containing peptide has been de novo designed and its crystal structure determined. The apolar peptide folds into a helical hairpin supersecondary structure with two right-handed helices, connected by a tetraglycine linker. The helices of the hairpin interact with each other through a combination of C-H.O and N-H.O hydrogen bonds. The folding of the apolar peptide has been realized without the help of either metal ions or disulphide bonds. A remarkable feature of the peptide is the unanticipated occurrence of an anion binding motif in the linker region, strikingly similar in conformation and function to the "nest" motif seen in several proteins. The observation supports the view for the possible emergence of rudimentary functions over short sequence stretches in the early peptides under prebiotic conditions.

About this Structure

1VRZ is a Protein complex structure of sequences from [1] with , and as ligands. This structure supersedes the now removed PDB entry 1Q4F. Full crystallographic information is available from OCA.

Reference

De novo design and characterization of a helical hairpin eicosapeptide; emergence of an anion receptor in the linker region., Rudresh, Ramakumar S, Ramagopal UA, Inai Y, Goel S, Sahal D, Chauhan VS, Structure. 2004 Mar;12(3):389-96. PMID:15016355

Page seeded by OCA on Thu Feb 21 15:38:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vrz"
Personal tools