1msg
From Proteopedia
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SOLUTION STRUCTURE OF GRO(SLASH)MELANOMA GROWTH STIMULATORY ACTIVITY DETERMINED BY 1H NMR SPECTROSCOPY
Contents |
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
Page seeded by OCA on Mon Nov 12 18:14:36 2007
