TY - JOUR
T1 - The ANK repeat
T2 - a ubiquitous motif involved in macromolecular recognition
AU - Michaely, Peter
AU - Bennett, Vann
PY - 1992/5
Y1 - 1992/5
N2 - Many proteins rely on stable, noncovalent interactions with other macromolecules to perform their function. The identification of a repeated sequence motif, the ANK repeat, in diverse proteins whose common function involves binding to other proteins indicates one way nature may achieve a wide range of protein-protein interactions. In this article, we describe evidence that these ANK repeats are involved in the specific recognition of proteins and possibly DNA, and present a model for the folding of the motif.
AB - Many proteins rely on stable, noncovalent interactions with other macromolecules to perform their function. The identification of a repeated sequence motif, the ANK repeat, in diverse proteins whose common function involves binding to other proteins indicates one way nature may achieve a wide range of protein-protein interactions. In this article, we describe evidence that these ANK repeats are involved in the specific recognition of proteins and possibly DNA, and present a model for the folding of the motif.
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U2 - 10.1016/0962-8924(92)90084-Z
DO - 10.1016/0962-8924(92)90084-Z
M3 - Article
C2 - 14731966
AN - SCOPUS:0026607234
VL - 2
SP - 127
EP - 129
JO - Trends in Cell Biology
JF - Trends in Cell Biology
SN - 0962-8924
IS - 5
ER -