Aromatic di-alanine repeats (AdAR) are structural motifs characteristic ofthe soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) family

Citation
F. Bruckert et al., Aromatic di-alanine repeats (AdAR) are structural motifs characteristic ofthe soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) family, PROTEINS, 45(1), 2001, pp. 40-46
Citations number
30
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PROTEINS-STRUCTURE FUNCTION AND GENETICS
ISSN journal
0887-3585 → ACNP
Volume
45
Issue
1
Year of publication
2001
Pages
40 - 46
Database
ISI
SICI code
0887-3585(20011001)45:1<40:ADR(AS>2.0.ZU;2-U
Abstract
The aromatic di-alanine repeat is a novel 12-amino acid-long motif constitu ting alternate small and large hydrophobic residues that mediate the close packing of alpha -helices. A hidden Markov model profile was constructed fr om the motifs initially described in Soluble N-ethyl maleimide-sensitive fa ctor attachment proteins (SNAP), a family of soluble proteins involved in i ntracellular membrane fusion. Scanning different sets of protein sequences showed unambiguously that this profile defines a structural motif independe nt of the tetratrico peptide repeat, another widespread alpha -helical moti f In addition to SNAP, aromatic di-alanine repeats are found in selective L IM homeodomain binding proteins (SLB) and in proteins from the Pyrococcus a nd Archaeoglobus prokaryotes. (C) 2001 Wiley-Liss, Inc.