This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1msg
From Proteopedia
(New page: 200px<br /> <applet load="1msg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1msg" /> '''SOLUTION STRUCTURE OF GRO(SLASH)MELANOMA GR...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1msg.gif|left|200px]]<br /> | + | [[Image:1msg.gif|left|200px]]<br /><applet load="1msg" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1msg" size=" | + | |
caption="1msg" /> | caption="1msg" /> | ||
'''SOLUTION STRUCTURE OF GRO(SLASH)MELANOMA GROWTH STIMULATORY ACTIVITY DETERMINED BY 1H NMR SPECTROSCOPY'''<br /> | '''SOLUTION STRUCTURE OF GRO(SLASH)MELANOMA GROWTH STIMULATORY ACTIVITY DETERMINED BY 1H NMR SPECTROSCOPY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional solution structure of the growth-related | + | 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== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1MSG 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:// | + | 1MSG 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=1MSG OCA]. |
==Reference== | ==Reference== | ||
| Line 18: | Line 17: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Clark-Lewis, I.]] | [[Category: Clark-Lewis, I.]] | ||
| - | [[Category: Kim, K | + | [[Category: Kim, K S.]] |
| - | [[Category: Sykes, B | + | [[Category: Sykes, B D.]] |
[[Category: cytokine (chemotactic)]] | [[Category: cytokine (chemotactic)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:35 2008'' |
Revision as of 11:58, 21 February 2008
|
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 Thu Feb 21 13:58:35 2008
