1yug
From Proteopedia
(New page: 200px<br /> <applet load="1yug" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yug" /> '''TYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR,...) |
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'''TYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR, 15 MODELS AFTER ECEPP/3 ENERGY MINIMIZATION'''<br /> | '''TYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR, 15 MODELS AFTER ECEPP/3 ENERGY MINIMIZATION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YUG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1YUG is a [http://en.wikipedia.org/wiki/Single_protein 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=1YUG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: growth factor]] | [[Category: growth factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:12:53 2008'' |
Revision as of 15:12, 15 February 2008
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TYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR, 15 MODELS AFTER ECEPP/3 ENERGY MINIMIZATION
Overview
Human type-alpha transforming growth factor (hTGF alpha) is a small, mitogenic protein containing 50 amino acids and 3 disulfide bonds. Homo-, and heteronuclear NMR spectra were used to determine nearly complete, sequence-specific 1H and 15N resonance assignments for hTGF alpha under, three conditions: pH 6.5 and a temperature of 10 degrees C, pH 6.5 and a, temperature of 30 degrees C, and pH 3.5 and a temperature of 30 degrees C., The 15N-enriched samples of hTGF alpha allowed determination of many, 3J(HN-H alpha) vicinal coupling constants. Solution structures of human, type-alpha transforming growth factor (hTGF alpha) at pH 6.5 and a, temperature of 10 degrees C were determined from NMR data using molecular, structure generation calculations and restrained energy minimization., These structures are based on 425 conformational constraints, including, 357 NOE-derived upper-bound distance constraints, constraints on the, ranges of 26 dihedral angles based on measurements of vicinal coupling, constants, 42 upper- and lower-bound constraints associated with 6, hydrogen bonds and 3 disulfide bonds, and several stereospecific 1H, resonance assignments. The overall structure is similar to that described, recently for hTGF alpha by other groups [Kline et al. (1990) Biochemistry, 29, 7805-7813; Harvey et al. (1991). Eur. J. Biochem. 198, 555-562], but, there are differences in some structural details. The resonance, frequencies, vicinal coupling constants, and NOEs form the basis for, comparisons of the solution structure of hTGF alpha at neutral and acidic, pH. At pH 3.5 the protein structure is partially disordered, with most of, the hydrogen-bonded backbone structure still intact. The hTGF alpha, structure is also compared with that of murine epidermal growth factor., Coordinates for the set of hTGF alpha structures described in this paper, have been deposited in the Protein Data Bank.
About this Structure
1YUG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints., Moy FJ, Li YC, Rauenbuehler P, Winkler ME, Scheraga HA, Montelione GT, Biochemistry. 1993 Jul 27;32(29):7334-53. PMID:8338831
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