1AXI

STRUCTURAL PLASTICITY AT THE HGH:HGHBP INTERFACE

1AXI の概要

• エントリーDOI: 10.2210/pdb1axi/pdb
• 分子名称: GROWTH HORMONE, GROWTH HORMONE RECEPTOR, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: complex (hormone-receptor), complex (hormone-receptor) complex, complex (hormone/receptor)
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: 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
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49349.44

構造登録者

Atwell, S.,Ultsch, M.,De Vos, A.M.,Wells, J.A. (登録日: 1997-10-15, 公開日: 1998-01-28, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)