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1hae

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{{STRUCTURE_1hae| PDB=1hae | SCENE= }}
{{STRUCTURE_1hae| PDB=1hae | SCENE= }}
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'''HEREGULIN-ALPHA EPIDERMAL GROWTH FACTOR-LIKE DOMAIN, NMR, 20 STRUCTURES'''
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===HEREGULIN-ALPHA EPIDERMAL GROWTH FACTOR-LIKE DOMAIN, NMR, 20 STRUCTURES===
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==Overview==
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The solution structure of the 63-residue heregulin-alpha (HRG-alpha) epidermal growth factor (EGF)-like domain, corresponding to residues 177-239 of HRG-alpha, has been determined to high resolution using data from two-dimensional and three-dimensional homo- and heteronuclear NMR spectroscopy. The structure is based on a total of 887 internuclear distance and dihedral restraints derived from data obtained using unlabeled and uniformly 15N-labeled protein samples, at pH 4.5, 20 degrees C. A total of 20 structures were calculated using a hybrid distance geometry-simulated annealing approach with the program DGII, followed by restrained molecular dynamics using the program DISCOVER. The average maximum violations are 0.12 +/- 0.01 angstroms and 1.4 +/- 0.3 degrees for distance and dihedral restraints, respectively. The backbone (N,C(alpha),C) atomic rms distribution about the mean coordinates for residues 3-23 and 31-49 is 0.29 +/- 0/07 angstroms. The N-and C-terminal residues (1-2 and 50-63) and 24-30 are disordered. Comparison of the HRG-alpha EGF-like domain structure with the previously determined structure of human EGF [Hommel et al. (1992) J. Mol. Biol. 227, 271-282] reveals a high degree of structural similarity; excluding the N-terminal region (residues 1-13), the disordered phi-loop region (residues 24-30) that contains a three-residue insertion in HRG-alpha relative to hEGF, and the disordered C-terminal region (residues 50-63), the C(alpha) alignment between the HRG-alpha and hEGF minimized mean structures has a rms difference of approximately 1 angstrom. In HRG-alpha the N-terminal residues 2-6 form a well-defined beta strand rather than being disordered as found for hEGF. This structural difference correlates with functional data which suggest that the N-terminal region of the HRG-alpha EGF-like domain is responsible for the observed receptor specificity differences between HRG-alpha and EGF.
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{{ABSTRACT_PUBMED_8639490}}
==About this Structure==
==About this Structure==
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1HAE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HAE OCA].
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1HAE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HAE OCA].
==Reference==
==Reference==
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[[Category: Skelton, N J.]]
[[Category: Skelton, N J.]]
[[Category: Growth factor]]
[[Category: Growth factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:38:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 07:53:52 2008''

Revision as of 04:53, 1 July 2008

Image:1hae.png

Template:STRUCTURE 1hae

HEREGULIN-ALPHA EPIDERMAL GROWTH FACTOR-LIKE DOMAIN, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 8639490

About this Structure

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

Reference

High-resolution solution structure of the EGF-like domain of heregulin-alpha., Jacobsen NE, Abadi N, Sliwkowski MX, Reilly D, Skelton NJ, Fairbrother WJ, Biochemistry. 1996 Mar 19;35(11):3402-17. PMID:8639490

Page seeded by OCA on Tue Jul 1 07:53:52 2008

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