1AXI

STRUCTURAL PLASTICITY AT THE HGH:HGHBP INTERFACE

Summary for 1AXI

• Entry DOI: 10.2210/pdb1axi/pdb
• Descriptor: GROWTH HORMONE, GROWTH HORMONE RECEPTOR, SULFATE ION, ... (4 entities in total)
• Functional Keywords: complex (hormone-receptor), complex (hormone-receptor) complex, complex (hormone/receptor)
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P01241; Cell membrane; Single-pass type I membrane protein. Isoform 2: Cell membrane; Single-pass type I membrane protein. Growth hormone-binding protein: Secreted: P10912
• Total number of polymer chains: 2
• Total formula weight: 49349.44

Authors

Atwell, S.,Ultsch, M.,De Vos, A.M.,Wells, J.A. (deposition date: 1997-10-15, release date: 1998-01-28, Last modification date: 2024-11-20)

Primary citation

Atwell, S.,Ultsch, M.,De Vos, A.M.,Wells, J.A.
Structural plasticity in a remodeled protein-protein interface.
Science, 278:1125-1128, 1997

PubMed Abstract: 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.

PubMed: 9353194
DOI: 10.1126/science.278.5340.1125

Experimental method

X-RAY DIFFRACTION (2.1 Å)