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PDBsum entry 1vhh
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Signalling protein
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PDB id
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1vhh
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References listed in PDB file
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Key reference
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Title
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A potential catalytic site revealed by the 1.7-A crystal structure of the amino-Terminal signalling domain of sonic hedgehog.
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Authors
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T.M.Hall,
J.A.Porter,
P.A.Beachy,
D.J.Leahy.
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Ref.
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Nature, 1995,
378,
212-216.
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PubMed id
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Abstract
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Within the past few years, members of the hedgehog (hh) family of secreted
signalling proteins have emerged as the primary signals generated by certain
embryonic patterning centres. In vertebrate embryos, for example, sonic hedgehog
expression in the notochord appears to be responsible for the local and
long-range induction of ventral cell types within the neural tube and somites
(reviewed in refs 1, 2). Protein products encoded by hh family members are
synthesized as precursors that undergo autoprocessing to generate an
amino-terminal domain that appears to be responsible for both local and
long-range signalling activities, and a carboxy-terminal domain that contains
the autoprocessing activity. As part of an effort to understand how hh family
members participate in cell-to-cell signalling, we have determined and report
here the crystal structure at 1.7 A of the amino-terminal domain of murine Sonic
hedgehog (Shh-N). The structure revealed a tetrahedrally coordinated zinc ion
that appears to be structurally analogous to the zinc coordination sites of zinc
hydrolases, such as thermolysin and carboxypeptidase A. This previously
unsuspected catalytic site represents a distinct activity from the
autoprocessing activity that resides in the carboxy-terminal domain.
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