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... > Chemical Phenomena > Biochemical Phenomena > Molecular Structure > Molecular Conformation > Protein Conformation > Protein Structural Elements > Protein Domains > Protein Interaction Domains and Motifs > Ankyrin Repeat
... > Chemical Phenomena > Biochemical Phenomena > Molecular Structure > Molecular Conformation > Protein Conformation > Protein Structure, Tertiary > Protein Domains > Protein Interaction Domains and Motifs > Ankyrin Repeat
... > Chemical Phenomena > Biochemical Phenomena > Molecular Structure > Molecular Conformation > Protein Conformation > Protein Structural Elements > Amino Acid Motifs > Ankyrin Repeat
... > Chemical Phenomena > Biochemical Phenomena > Molecular Structure > Molecular Conformation > Protein Conformation > Protein Structure, Secondary > Amino Acid Motifs > Ankyrin Repeat
... > Chemical Phenomena > Biochemical Phenomena > Molecular Structure > Molecular Conformation > Protein Conformation > Protein Structural Elements > Repetitive Sequences, Amino Acid > Ankyrin Repeat
... > Chemical Phenomena > Biochemical Phenomena > Molecular Structure > Amino Acid Sequence > Repetitive Sequences, Amino Acid > Ankyrin Repeat
... > Information Science > Information Services > Documentation > Molecular Sequence Data > Amino Acid Sequence > Repetitive Sequences, Amino Acid > Ankyrin Repeat

Terme préférentiel

Ankyrin Repeat  

Type

  • mesh:Descriptor

Définition

  • Protein motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating sequence of 33-amino acids was discovered in ANKYRIN where it is involved in interaction with the anion exchanger (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE). Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions.

Concept générique

Concepts associés

Synonyme(s)

  • ANK Repeat
  • Ankyrin Repeats

Qualificatif(s) autorisé(s)

Traductions

URI

http://data.loterre.fr/ark:/67375/JVR-PWMV44VW-L

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RDF/XML TURTLE JSON-LD Date de création 13/05/1992, dernière modification le 27/05/2016