1axi
STRUCTURAL PLASTICITY AT THE HGH:HGHBP INTERFACE
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| , resolution 2.1Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
Remodeling of the interface between human growth hormone (hGH) and the extracellular domain of its receptor was studied by deleting a critical tryptophan residue (at position 104) in the receptor, creating a large cavity, and selecting a pentamutant of hGH by phage display that fills the cavity and largely restores binding affinity. A 2.1 A resolution x-ray structure of the mutant complex showed that the receptor cavity was filled by selected hydrophobic mutations of hGH. Large structural rearrangements occurred in the interface at sites that were distant from the mutations. Such plasticity may be a means for protein-protein interfaces to adapt to mutations as they coevolve.
About this StructureAbout this Structure
1AXI is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural plasticity in a remodeled protein-protein interface., Atwell S, Ultsch M, De Vos AM, Wells JA, Science. 1997 Nov 7;278(5340):1125-8. PMID:9353194
Page seeded by OCA on Sun Mar 30 18:49:25 2008