1vrz

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[[Image:1vrz.gif|left|200px]]
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{{STRUCTURE_1vrz| PDB=1vrz | SCENE= }}
{{STRUCTURE_1vrz| PDB=1vrz | SCENE= }}
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'''Helix turn helix motif'''
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===Helix turn helix motif===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15016355 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15016355}}
==About this Structure==
==About this Structure==
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[[Category: Sahal, D.]]
[[Category: Sahal, D.]]
[[Category: Hth,helix-turn-helix motif]]
[[Category: Hth,helix-turn-helix motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:51:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:59:04 2008''

Revision as of 17:59, 27 July 2008

Template:STRUCTURE 1vrz

Helix turn helix motif

Template:ABSTRACT PUBMED 15016355

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

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