1msg
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1msh|1MSH]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1msg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1msg OCA], [http://www.ebi.ac.uk/pdbsum/1msg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1msg RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600835 600835]], Osteogenesis imperfecta, type VIII OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=610339 610339]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: cytokine (chemotactic)]] | [[Category: cytokine (chemotactic)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:20:35 2008'' |
Revision as of 19:20, 30 March 2008
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| Related: | 1MSH
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
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 Sun Mar 30 22:20:35 2008
