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

Proteins. 2001 Oct 1;45(1):40-6. doi: 10.1002/prot.1121.

Abstract

The aromatic di-alanine repeat is a novel 12-amino acid-long motif constituting alternate small and large hydrophobic residues that mediate the close packing of alpha-helices. A hidden Markov model profile was constructed from the motifs initially described in Soluble N-ethyl maleimide-sensitive factor attachment proteins (SNAP), a family of soluble proteins involved in intracellular membrane fusion. Scanning different sets of protein sequences showed unambiguously that this profile defines a structural motif independent of the tetratrico peptide repeat, another widespread alpha-helical motif. In addition to SNAP, aromatic di-alanine repeats are found in selective LIM homeodomain binding proteins (SLB) and in proteins from the Pyrococcus and Archaeoglobus prokaryotes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alanine / chemistry*
  • Alanine / metabolism*
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism
  • Computer Simulation
  • Crystallography, X-Ray
  • Databases, Factual
  • Expressed Sequence Tags
  • Markov Chains
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Models, Molecular
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Repetitive Sequences, Amino Acid*
  • Saccharomyces cerevisiae Proteins*
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Vesicular Transport Proteins*

Substances

  • Carrier Proteins
  • Membrane Proteins
  • SEC17 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Vesicular Transport Proteins
  • Alanine