Conformational and sequence signatures in β helix proteins

Iengar, Prathima ; Joshi, N. V. ; Balaram, Padmanabhan (2006) Conformational and sequence signatures in β helix proteins Structure, 14 (3). pp. 529-542. ISSN 0969-2126

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Official URL: http://www.cell.com/structure/retrieve/pii/S096921...

Related URL: http://dx.doi.org/10.1016/j.str.2005.11.021

Abstract

β helix proteins are characterized by a repetitive fold, in which the repeating unit is a β-helical coil formed by three strand segments linked by three loop segments. Using a data set of left- and right-handed β helix proteins, we have examined conformational features at equivalent positions in successive coils. This has provided insights into the conformational rules that the proteins employ to fold into β helices. Left-handed β helices attain their equilateral prism fold by incorporating "corners" with the conformational sequence PII-PIIL-PII, which imposes sequence restrictions, resulting in the first and third PII residues often being G and a small, uncharged residue (V, A, S, T, C), respectively. Right-handed β helices feature mid-sized loops (4, 5, or 6 residues) of conserved conformation, but not of conserved sequence; they also display an α-helical residue at the C-terminal end of L2 loops. Backbone conformational parameters (Φ,Ψ) that permit the formation of continuous, loopless β helices (Perutz nanotubes) have also been investigated.

Item Type:Article
Source:Copyright of this article belongs to Cell Press Inc.
ID Code:4560
Deposited On:14 Oct 2010 05:07
Last Modified:16 May 2016 15:11

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