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The ankyrin repeat as molecular architecture for protein recognition
Author(s) -
Mosavi Leila K.,
Cammett Tobin J.,
Desrosiers Daniel C.,
Peng Zhengyu
Publication year - 2004
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.03554604
Subject(s) - ankyrin repeat , ankyrin , computational biology , protein folding , protein structure , structural motif , biology , folding (dsp implementation) , microbiology and biotechnology , biophysics , genetics , biochemistry , gene , engineering , electrical engineering
The ankyrin repeat is one of the most frequently observed amino acid motifs in protein databases. This protein–protein interaction module is involved in a diverse set of cellular functions, and consequently, defects in ankyrin repeat proteins have been found in a number of human diseases. Recent biophysical, crystallographic, and NMR studies have been used to measure the stability and define the various topological features of this motif in an effort to understand the structural basis of ankyrin repeat‐mediated protein–protein interactions. Characterization of the folding and assembly pathways suggests that ankyrin repeat domains generally undergo a two‐state folding transition despite their modular structure. Also, the large number of available sequences has allowed the ankyrin repeat to be used as a template for consensus‐based protein design. Such projects have been successful in revealing positions responsible for structure and function in the ankyrin repeat as well as creating a potential universal scaffold for molecular recognition.