1ROD: CHIMERIC PROTEIN OF INTERLEUKIN 8 AND HUMAN MELANOMA GROWTH STIMULATING ACTIVITY PROTEIN, NMR

Citation:
Abstract
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.
PDB ID: 1RODDownload
MMDB ID: 4690
PDB Deposition Date: 1995/11/24
Updated in MMDB: 1998/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 1ROD
Label Count Molecule
Proteins (2 molecules)
2
Chimeric Protein of Interleukin 8 and Human Melanoma Growth Stimulating Activity Protein(Gene symbol: CXCL8)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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