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'''SOLUTION STRUCTURE OF GRO(SLASH)MELANOMA GROWTH STIMULATORY ACTIVITY DETERMINED BY 1H NMR SPECTROSCOPY''' | {{Structure | ||
|PDB= 1msg |SIZE=350|CAPTION= <scene name='initialview01'>1msg</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''SOLUTION STRUCTURE OF GRO(SLASH)MELANOMA GROWTH STIMULATORY ACTIVITY DETERMINED BY 1H NMR SPECTROSCOPY''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MSG is a [ | 1MSG 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=1MSG OCA]. | ||
==Reference== | ==Reference== | ||
Solution structure of GRO/melanoma growth stimulatory activity determined by 1H NMR spectroscopy., Kim KS, Clark-Lewis I, Sykes BD, J Biol Chem. 1994 Dec 30;269(52):32909-15. PMID:[http:// | Solution structure of GRO/melanoma growth stimulatory activity determined by 1H NMR spectroscopy., Kim KS, Clark-Lewis I, Sykes BD, J Biol Chem. 1994 Dec 30;269(52):32909-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7806518 7806518] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cytokine (chemotactic)]] | [[Category: cytokine (chemotactic)]] | ||
''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 12:47:36 2008'' | ||
Revision as of 10:47, 20 March 2008
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SOLUTION STRUCTURE OF GRO(SLASH)MELANOMA GROWTH STIMULATORY ACTIVITY DETERMINED BY 1H NMR SPECTROSCOPY
Overview
The three-dimensional solution structure of the growth-related protein-alpha/melanoma growth stimulatory activity (GRO/MGSA) has been solved by two-dimensional 1H nuclear magnetic resonance spectroscopy. The GRO/MGSA monomer consists of an NH2-terminal loop, a three-stranded antiparallel beta-sheet, and a COOH-terminal alpha-helix. Dimerization, which is apparent under the experimental conditions used (2 mM, pH 5.10, 30 degrees C), results in a six-stranded antiparallel beta-sheet and a pair of helices with 2-fold symmetry. While the basic fold is similar to that seen for interleukin-8 (IL-8) (Clore, G. M., Appella, E., Yamada, M., Matsushima, K., and Gronenborn, A. M. (1990) Biochemistry, 29, 1689-1696), there are differences in the ELR motif (residues 6-8), the turn involving residues 31-36, which is linked to the NH2-terminal region through the 9-35 disulfide bond. The most significant differences are in the NH2-terminal loop (residues 12-23). In IL-8, all the corresponding regions have been shown to be required for receptor binding (Clark-Lewis, I., Dewald, B., Loetscher, M., Moser, B., and Baggiolini, M. (1994) J. Biol. Chem. 269, 16075-16081). The structural differences thus have been identified between GRO/MGSA and IL-8 could contribute to their different receptor binding specificities.
Disease
Known diseases associated with this structure: AIDS, resistance to OMIM:[600835], Osteogenesis imperfecta, type VIII OMIM:[610339]
About this Structure
1MSG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of GRO/melanoma growth stimulatory activity determined by 1H NMR spectroscopy., Kim KS, Clark-Lewis I, Sykes BD, J Biol Chem. 1994 Dec 30;269(52):32909-15. PMID:7806518
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