Abstract
The phox homology (PX) domain is a novel protein module containing a conserved proline-rich motif. We have shown that the PX domain isolated from the human p47phox protein, a soluble subunit of phagocyte NADPH oxidase, binds specifically to the C-terminal SH3 domain derived from the same protein. The solution structure of p47 PX has an alpha + beta structure with a novel folding motif topology and reveals that the proline-rich motif is presented on the molecular surface for easy recognition by the SH3 domain. The proline-rich motif of p47 PX in the free state adopts a distorted left-handed polyproline type II helix conformation.
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Binding Sites
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Conserved Sequence
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Humans
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Models, Molecular
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Molecular Sequence Data
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NADPH Oxidases / chemistry
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Nuclear Magnetic Resonance, Biomolecular
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Phosphoproteins / chemistry*
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Phosphoproteins / metabolism*
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Proline / metabolism
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Protein Binding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Protein Subunits
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Proto-Oncogene Proteins pp60(c-src) / chemistry
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Sequence Alignment
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src Homology Domains*
Substances
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Phosphoproteins
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Protein Subunits
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Recombinant Fusion Proteins
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Proline
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NADPH Oxidases
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neutrophil cytosolic factor 1
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Proto-Oncogene Proteins pp60(c-src)