 |
PDBsum entry 1ip0
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Hormone/growth factor
|
PDB id
|
|
|
|
1ip0
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Solution structure of betacellulin, A new member of egf-Family ligands.
|
 |
|
Authors
|
 |
K.Miura,
H.Doura,
T.Aizawa,
H.Tada,
M.Seno,
H.Yamada,
K.Kawano.
|
 |
|
Ref.
|
 |
Biochem Biophys Res Commun, 2002,
294,
1040-1046.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
The solution structure of the EGF-like domain of betacellulin (BTCe), a newly
discovered member of the epidermal growth factor (EGF) family, has been
determined using two-dimensional nuclear magnetic resonance spectroscopy. This
is the first report to identify the solution structure of the EGF-family ligand
monomers that interact with both ErbB-1 and ErbB-4. The solution structure of
BTCe was calculated using 538 NMR-derived restraints. The overall structure of
BTCe was stabilized by three disulfide bonds, a hydrophobic core, and 23
hydrogen bonds. It appears that BTCe is comprised of five beta-strands and one
short 3(10) helical turn. The secondary structural elements of BTCe are
basically similar to those of the other EGF-family proteins, except that several
significant variations of the structural properties were found. It is suggested
that the structural variations between BTCe and the other EGF-family ligands may
affect the specific receptor-recognition properties of EGF-family ligands.
|
 |
|
|
|
|
 |