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PDBsum entry 1kjs
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Cell adhesion
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PDB id
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1kjs
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References listed in PDB file
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Key reference
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Title
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Structural definition of the c5a c terminus by two-Dimensional nuclear magnetic resonance spectroscopy.
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Authors
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X.Zhang,
W.Boyar,
M.J.Toth,
L.Wennogle,
N.C.Gonnella.
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Ref.
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Proteins, 1997,
28,
261-267.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above were
obtained from the PDBe's
server.
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Abstract
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The serum glycoprotein C5a, which is derived from the proteolytic cleavage of
complement protein C5, has been implicated in the pathogenesis of a number of
inflammatory and allergic conditions. Because C5a induces an inflammatory
response upon binding to a specific receptor, structural and mutagenesis studies
were carried out to gain a better understanding of this binding interaction.
These studies led to the first structural definition of the C terminus of
recombinant human (rh)-C5a, determined by two-dimensional nuclear magnetic
resonance (NMR) spectroscopy. Our results show that the C terminus adopts an
alpha-helical conformation spanning residues 69 to 74, while the core domain
exists as an antiparallel alpha-helical bundle. This C-terminal helix is
connected to the core by a short loop that orients Arg 74 adjacent to Arg 62.
Point mutation analysis had already revealed that residues 62 and 74
significantly contribute to agonist activity and receptor binding. Correlation
of the C5a tertiary structure with mutational analyses clarifies the
significance of the functional and binding properties of Arg 62 and suggests
that both Arg 62 and Arg 74 interact at the same binding site on the receptor.
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