Helix packing of leucine-rich peptides: A parallel leucine ladder in the structure of Boc-Aib-Leu-Aib-Aib-Leu-Leu-Leu-Aib-Leu-Aib-OMe

Karle, Isabella L. ; Flippen-Anderson, Judith L. ; Sukumar, M. ; Balaram, P. (1992) Helix packing of leucine-rich peptides: A parallel leucine ladder in the structure of Boc-Aib-Leu-Aib-Aib-Leu-Leu-Leu-Aib-Leu-Aib-OMe Proteins: Structure, Function, and Bioinformatics, 12 (4). pp. 324-330. ISSN 0887-3585

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Official URL: http://www3.interscience.wiley.com/journal/1076110...

Related URL: http://dx.doi.org/10.1002/prot.340120404

Abstract

The packing of peptide helices in crystals of the leucine-rich decapeptide Boc-Aib-Leu-Aib-Aib-Leu-Leu-Leu-Aib-Leu-Aib-OMe provides an example of ladder-like leucylleucyl interactions between neighboring molecules. The peptide molecule forms a helix with five 5→1 hydrogen bonds and two 4→1 hydrogen bonds near the C terminus. Three head-to-tail NH c O = C hydrogen bonds between helices form continuous columns of helices in the crystal. The helicial columns associate in an antiparallel fashion, except for the association of Leu Leu side chains, which occurs along the diagonal of the cell where the peptide helices are parallel. The peptide, with formula C56H102N10O13, crystallizes in space group P212121 with Z = 4 and cell parameters a = 16.774(3) Å, b = 20.032(3) Å and c = 20.117(3) Å; overall agreement factor R = 10.7% for 2014 data with |Fobs| <3σ(F); resolution 1.0 Å.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons, Inc.
Keywords:X-ray Diffraction Analysis; Hydrogen Bonds; Peptide Conformation; 310/α-helix Transition; Antiparallel Helix Packing; Leucyl-leucyl Interaction
ID Code:4739
Deposited On:18 Oct 2010 06:55
Last Modified:16 May 2016 15:21

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