TY - JOUR
T1 - The structure of GABPα/β
T2 - An ETS domain-ankyrin repeat heterodimer bound to DNA
AU - Batchelor, Adrian H.
AU - Piper, Derek E.
AU - Charles De La Brousse, Fabienne
AU - McKnight, Steven L.
AU - Wolberger, Cynthia
PY - 1998/2/13
Y1 - 1998/2/13
N2 - GA-binding protein (GABP) is a transcriptional regulator composed of two structurally dissimilar subunits. The α subunit contains a DNA-binding domain that is a member of the ETS family, whereas the α subunit contains a series of ankyrin repeats. The crystal structure of a ternary complex containing a GABPα/β ETS domain-ankyrin repeat heterodimer bound to DNA was determined at 2.15 angstrom resolution. The structure shows how an ETS domain protein can recruit a partner protein using both the ETS domain and a carboxyl-terminal extension and provides a view of an extensive protein- protein interface formed by a set of ankyrin repeats. The structure also reveals how the GABPα ETS domain binds to its core GGA DNA-recognition motif.
AB - GA-binding protein (GABP) is a transcriptional regulator composed of two structurally dissimilar subunits. The α subunit contains a DNA-binding domain that is a member of the ETS family, whereas the α subunit contains a series of ankyrin repeats. The crystal structure of a ternary complex containing a GABPα/β ETS domain-ankyrin repeat heterodimer bound to DNA was determined at 2.15 angstrom resolution. The structure shows how an ETS domain protein can recruit a partner protein using both the ETS domain and a carboxyl-terminal extension and provides a view of an extensive protein- protein interface formed by a set of ankyrin repeats. The structure also reveals how the GABPα ETS domain binds to its core GGA DNA-recognition motif.
UR - http://www.scopus.com/inward/record.url?scp=0032512459&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032512459&partnerID=8YFLogxK
U2 - 10.1126/science.279.5353.1037
DO - 10.1126/science.279.5353.1037
M3 - Article
C2 - 9461436
AN - SCOPUS:0032512459
SN - 0036-8075
VL - 279
SP - 1037
EP - 1041
JO - Science
JF - Science
IS - 5353
ER -