1msg

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{{Structure
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The line below this paragraph, containing "STRUCTURE_1msg", creates the "Structure Box" on the page.
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|RELATEDENTRY=[[1msh|1MSH]]
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|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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'''SOLUTION STRUCTURE OF GRO(SLASH)MELANOMA GROWTH STIMULATORY ACTIVITY DETERMINED BY 1H NMR SPECTROSCOPY'''
'''SOLUTION STRUCTURE OF GRO(SLASH)MELANOMA GROWTH STIMULATORY ACTIVITY DETERMINED BY 1H NMR SPECTROSCOPY'''
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[[Category: Kim, K S.]]
[[Category: Kim, K S.]]
[[Category: Sykes, B D.]]
[[Category: Sykes, B D.]]
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[[Category: cytokine (chemotactic)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:40:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:20:35 2008''
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Revision as of 22:40, 2 May 2008

Template:STRUCTURE 1msg

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 Sat May 3 01:40:11 2008

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