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==Overview==

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.

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.

==About this Structure==

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[[Category: egf-like fold]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:19 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 22: / Line 22: @@
 [[Category: egf-like fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:02:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:19 2008''