1vrz
From Proteopedia
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[[Image:1vrz.gif|left|200px]] | [[Image:1vrz.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_1vrz| PDB=1vrz | SCENE= }} | |
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'''Helix turn helix motif''' | '''Helix turn helix motif''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1q4f 1q4f]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRZ OCA]. | |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/15016355 15016355] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15016355 15016355] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Inai, Y.]] | [[Category: Inai, Y.]] | ||
[[Category: Ramagopal, U A.]] | [[Category: Ramagopal, U A.]] | ||
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[[Category: Rudresh]] | [[Category: Rudresh]] | ||
[[Category: Sahal, D.]] | [[Category: Sahal, D.]] | ||
| - | [[Category: | + | [[Category: Hth,helix-turn-helix motif]] |
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Revision as of 09:51, 3 May 2008
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
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 Sat May 3 12:51:10 2008
