1haf
From Proteopedia
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| - | [[Image:1haf.gif|left|200px]] | + | [[Image:1haf.gif|left|200px]] |
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| - | '''HEREGULIN-ALPHA EPIDERMAL GROWTH FACTOR-LIKE DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE''' | + | {{Structure |
| + | |PDB= 1haf |SIZE=350|CAPTION= <scene name='initialview01'>1haf</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
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| + | '''HEREGULIN-ALPHA EPIDERMAL GROWTH FACTOR-LIKE DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HAF is a [ | + | 1HAF 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=1HAF OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8639490 8639490] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: growth factor]] | [[Category: growth factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:34:29 2008'' |
Revision as of 09:34, 20 March 2008
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HEREGULIN-ALPHA EPIDERMAL GROWTH FACTOR-LIKE DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Fibromatosis, gingival, 2 OMIM:[605544], Schizophrenia, susceptibility to OMIM:[142445]
About this Structure
1HAF is a Single protein structure of sequence from Homo sapiens. Full crystallographic 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
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