Journal article
Aromatic di‐alanine repeats (AdAR) are structural motifs characteristic of the soluble N‐ethylmaleimide‐sensitive factor attachment protein (SNAP) family
Proteins, structure, function, and bioinformatics, Vol.45(1), pp.40-46
10/01/2001
DOI: 10.1002/prot.1121
PMID: 11536358
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 α‐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 α‐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. Proteins 2001;45:40–46. © 2001 Wiley‐Liss, Inc.
Details
- Title: Subtitle
- Aromatic di‐alanine repeats (AdAR) are structural motifs characteristic of the soluble N‐ethylmaleimide‐sensitive factor attachment protein (SNAP) family
- Creators
- Franz BruckertThomas CasavantMichel Satre
- Resource Type
- Journal article
- Publication Details
- Proteins, structure, function, and bioinformatics, Vol.45(1), pp.40-46
- Publisher
- John Wiley & Sons, Inc; New York
- DOI
- 10.1002/prot.1121
- PMID
- 11536358
- ISSN
- 0887-3585
- eISSN
- 1097-0134
- Number of pages
- 7
- Grant note
- Université Joseph Fourier‐Grenoble Centre National de la Recherche Scientifique Commissariat à l'Energie Atomique
- Language
- English
- Date published
- 10/01/2001
- Academic Unit
- Roy J. Carver Department of Biomedical Engineering; Electrical and Computer Engineering
- Record Identifier
- 9984064568402771
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