1rod: Difference between revisions

Revision as of 15:52, 21 February 2008

CHIMERIC PROTEIN OF INTERLEUKIN 8 AND HUMAN MELANOMA GROWTH STIMULATING ACTIVITY PROTEIN, NMR

OverviewOverview

A 72-amino-acid chimeric protein, Chi1, was constructed from the N-terminal part of interleukin 8, IL-8-(1-53), and the C-terminal part of melanoma growth stimulatory activity, MGSA-(54-72). Chi1 protein showed receptor-binding specificity and biological activity similar, but not identical to IL-8 and decidedly different from MGSA. The structure of Chi1 was determined in solution by two-dimensional NMR and molecular-dynamics calculations. The structure resembled the structures of MGSA and IL-8 closely, containing a triple-stranded beta-sheet in the IL-8 part and an amphipathic alpha-helix in the MGSA part. Chi1 formed dimers at millimolar concentrations via the first strand from the N-terminus, analogous to IL-8 and MGSA. In contrast to the latter molecules, however, the alpha-helix of Chi1 did not pack against the beta-sheet part, but was an independent structural element. This structural difference could be explained mainly by the modulation of hydrophobic interactions between the helix and the rest of the protein in Chi1 as compared to IL-8 and MGSA. It is concluded that tight helix packing is not required for receptor binding and biological activity of Chi1.

About this StructureAbout this Structure

1ROD is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure and activity of a chimeric interleukin-8-melanoma-growth-stimulatory-activity protein., Sticht H, Auer M, Schmitt B, Besemer J, Horcher M, Kirsch T, Lindley IJ, Rosch P, Eur J Biochem. 1996 Jan 15;235(1-2):26-35. PMID:8631339

Page seeded by OCA on Thu Feb 21 14:52:56 2008

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OCA

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-[[Image:1rod.gif|left|200px]]<br /><applet load="1rod" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1rod" />
 '''CHIMERIC PROTEIN OF INTERLEUKIN 8 AND HUMAN MELANOMA GROWTH STIMULATING ACTIVITY PROTEIN, NMR'''<br />
 ==Overview==
-A 72-amino-acid chimeric protein, Chi1, was constructed from the, N-terminal part of interleukin 8, IL-8-(1-53), and the C-terminal part of, melanoma growth stimulatory activity, MGSA-(54-72). Chi1 protein showed, receptor-binding specificity and biological activity similar, but not, identical to IL-8 and decidedly different from MGSA. The structure of Chi1, was determined in solution by two-dimensional NMR and molecular-dynamics, calculations. The structure resembled the structures of MGSA and IL-8, closely, containing a triple-stranded beta-sheet in the IL-8 part and an, amphipathic alpha-helix in the MGSA part. Chi1 formed dimers at millimolar, concentrations via the first strand from the N-terminus, analogous to IL-8, and MGSA. In contrast to the latter molecules, however, the alpha-helix of, Chi1 did not pack against the beta-sheet part, but was an independent, structural element. This structural difference could be explained mainly, by the modulation of hydrophobic interactions between the helix and the, rest of the protein in Chi1 as compared to IL-8 and MGSA. It is concluded, that tight helix packing is not required for receptor binding and, biological activity of Chi1.
+A 72-amino-acid chimeric protein, Chi1, was constructed from the N-terminal part of interleukin 8, IL-8-(1-53), and the C-terminal part of melanoma growth stimulatory activity, MGSA-(54-72). Chi1 protein showed receptor-binding specificity and biological activity similar, but not identical to IL-8 and decidedly different from MGSA. The structure of Chi1 was determined in solution by two-dimensional NMR and molecular-dynamics calculations. The structure resembled the structures of MGSA and IL-8 closely, containing a triple-stranded beta-sheet in the IL-8 part and an amphipathic alpha-helix in the MGSA part. Chi1 formed dimers at millimolar concentrations via the first strand from the N-terminus, analogous to IL-8 and MGSA. In contrast to the latter molecules, however, the alpha-helix of Chi1 did not pack against the beta-sheet part, but was an independent structural element. This structural difference could be explained mainly by the modulation of hydrophobic interactions between the helix and the rest of the protein in Chi1 as compared to IL-8 and MGSA. It is concluded that tight helix packing is not required for receptor binding and biological activity of Chi1.
 ==About this Structure==
-ROD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ROD OCA].
+ROD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1ROD OCA].
 ==Reference==
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 [[Category: Horcher, M.]]
 [[Category: Kirsch, T.]]
-[[Category: Lindley, I.J.D.]]
+[[Category: Lindley, I J.D.]]
 [[Category: Roesch, P.]]
 [[Category: Schmitt, B.]]
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 [[Category: inflammatory response]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:45:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:56 2008''