 |
PDBsum entry 1wer
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Gtpase activation
|
PDB id
|
|
|
|
1wer
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of the gtpase-Activating domain of human p120gap and implications for the interaction with ras.
|
|
|
Authors
|
|
K.Scheffzek,
A.Lautwein,
W.Kabsch,
M.R.Ahmadian,
A.Wittinghofer.
|
|
|
Ref.
|
|
Nature, 1996,
384,
591-596.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Ras-related GTP-binding proteins function as molecular switches which cycle
between GTP-bound 'on'- and GDP-bound 'off'-states. GTP hydrolysis is the common
timing mechanism that mediates the return from the 'on' to the 'off'-state. It
is usually slow but can be accelerated by orders of magnitude upon interaction
with GTPase-activating proteins (GAPs). In the case of Ras, a major regulator of
cellular growth, point mutations are found in approximately 30% of human tumours
which render the protein unable to hydrolyse GTP, even in the presence of
Ras-GAPs. The first structure determination of a GTPase-activating protein
reveals the catalytically active fragment of the Ras-specific p120GAP (ref. 2),
GAP-334, as an elongated, exclusively helical protein which appears to represent
a novel protein fold. The molecule consists of two domains, one of which
contains all the residues conserved among different GAPs for Ras. From the
location of conserved residues around a shallow groove in the central domain we
can identify the site of interaction with Ras x GTP. This leads to a model for
the interaction between Ras and GAP that satisfies numerous biochemical and
genetic data on this important regulatory process.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Crystallization and preliminary X-Ray crystallographic study of the ras-Gtpase-Activating domain of human p120gap.
|
|
|
Authors
|
|
K.Scheffzek,
A.Lautwein,
A.Scherer,
S.Franken,
A.Wittinghofer.
|
|
|
Ref.
|
|
Proteins, 1997,
27,
315-318.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #2
|
|
|
Title
|
|
Molecular cloning of two types of gap complementary DNA from human placenta.
|
|
|
Authors
|
|
M.Trahey,
G.Wong,
R.Halenbeck,
B.Rubinfeld,
G.A.Martin,
M.Ladner,
C.M.Long,
W.J.Crosier,
K.Watt,
K.Koths.
|
|
|
Ref.
|
|
Science, 1988,
242,
1697-1700.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #3
|
|
|
Title
|
|
A cytoplasmic protein stimulates normal n-Ras p21 gtpase, But does not affect oncogenic mutants.
|
|
|
Authors
|
|
M.Trahey,
F.Mccormick.
|
|
|
Ref.
|
|
Science, 1987,
238,
542-545.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
