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FEBS Lett. 1993 Sep 20;330(3):302-6.

1H assignment and secondary structure determination of human melanoma growth stimulating activity (MGSA) by NMR spectroscopy.

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Department of Protein Engineering, Genentech Inc., South San Francisco, CA 94080-4990.


The solution structure of melanoma growth stimulating activity (MGSA) has been investigated using proton NMR spectroscopy. Sequential resonance assignments have been carried out, and elements of secondary structure have been identified on the basis of NOE, coupling constant, chemical shift, and amide proton exchange data. Long-range NOEs have established that MGSA is a dimer in solution. The secondary structure and dimer interface of MGSA appear to be similar to those found previously for the homologous chemokine interleukin-8 [Clore et al. (1990) Biochemistry 29, 1689-1696]. The MGSA monomer contains a three stranded anti-parallel beta-sheet arranged in a 'Greek-key' conformation, and a C-terminal alpha-helix (residues 58-69).

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