Zinc fingers (ZFs) are among the most structurally diverse protein domains. They interact
with nucleic acids, other proteins and lipids to facilitate a multitude of biological processes …

First described 15 years ago as a cysteine-rich sequence that was common to a small group
of homeodomain transcription factors, the LIM domain is now recognized as a tandem zinc …

Zinc ions are key structural components of a large number of proteins. The binding of zinc
stabilizes the folded conformations of domains so that they may facilitate interactions …

Chromosomal abnormalities in tumours were recognized at the end of the last century but
their significance has only recently become clear. Distinct translocations in leukaemias and …

The LIM‐only protein Lmo2, activated by chromosomal translocations in T‐cell leukaemias,
is normally expressed in haematopoiesis. It interacts with TAL1 and GATA‐1 proteins, but …

Paxillin is a multi-domain scaffold protein that localizes to the intracellular surface of sites of
cell adhesion to the extracellular matrix. Through the interactions of its multiple protein …

Molecular scaffold or adaptor proteins facilitate precise spatiotemporal regulation and
integration of multiple signaling pathways to effect the optimal cellular response to changes …

Like all retroviruses, the human immunodeficiency virus selectively packages two copies of
its unspliced RNA genome, both of which are utilized for strand-transfer-mediated …

The LIM domain is a zinc finger structure that is present in several types of proteins,
including homeodomain transcription factors, kinases and proteins that consist of several …

The LIM domain is a specialized double-zinc finger motif found in a variety of proteins, in
association with domains of divergent functions or forming proteins composed primarily of …