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PDBsum entry 3hhr
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Hormone/receptor
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PDB id
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3hhr
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Human growth hormone and extracellular domain of its receptor: crystal structure of the complex.
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Authors
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A.M.De vos,
M.Ultsch,
A.A.Kossiakoff.
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Ref.
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Science, 1992,
255,
306-312.
[DOI no: ]
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PubMed id
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Abstract
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Binding of human growth hormone (hGH) to its receptor is required for regulation
of normal human growth and development. Examination of the 2.8 angstrom crystal
structure of the complex between the hormone and the extracellular domain of its
receptor (hGHbp) showed that the complex consists of one molecule of growth
hormone per two molecules of receptor. The hormone is a four-helix bundle with
an unusual topology. The binding protein contains two distinct domains, similar
in some respects to immunoglobulin domains. The relative orientation of these
domains differs from that found between constant and variable domains in
immunoglobulin Fab fragments. Both hGHbp domains contribute residues that
participate in hGH binding. In the complex both receptors donate essentially the
same residues to interact with the hormone, even though the two binding sites on
hGH have no structural similarity. Generally, the hormone-receptor interfaces
match those identified by previous mutational analyses. In addition to the
hormone-receptor interfaces, there is also a substantial contact surface between
the carboxyl-terminal domains of the receptors. The relative extents of the
contact areas support a sequential mechanism for dimerization that may be
crucial for signal transduction.
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Secondary reference #1
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Title
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Crystals of the complex between human growth hormone and the extracellular domain of its receptor.
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Authors
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M.Ultsch,
A.M.De vos,
A.A.Kossiakoff.
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Ref.
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J Mol Biol, 1991,
222,
865-868.
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PubMed id
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Secondary reference #2
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Title
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Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule.
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Authors
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B.C.Cunningham,
M.Ultsch,
A.M.De vos,
M.G.Mulkerrin,
K.R.Clauser,
J.A.Wells.
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Ref.
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Science, 1991,
254,
821-825.
[DOI no: ]
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PubMed id
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