1ip0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==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==
==About this Structure==
Line 22: Line 22:
[[Category: egf-like fold]]
[[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''

Revision as of 11:14, 21 February 2008


1ip0

Drag the structure with the mouse to rotate

NMR STRUCTURE OF HUMAN BETACELLULIN-2

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.

About this Structure

1IP0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of betacellulin, a new member of EGF-family ligands., Miura K, Doura H, Aizawa T, Tada H, Seno M, Yamada H, Kawano K, Biochem Biophys Res Commun. 2002 Jun 28;294(5):1040-6. PMID:12074582

Page seeded by OCA on Thu Feb 21 13:14:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools