1axi

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spinqualitylabelsall models 1axi, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURAL PLASTICITY AT THE HGH:HGHBP INTERFACE

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known diseases associated with this structure: Growth hormone deficiency OMIM:[139250], Growth hormone deficiency, isolated, type IA OMIM:[139250], Growth hormone deficiency, isolated, type IB OMIM:[139250], Growth hormone deficiency, isolated, type II OMIM:[139250], Increased responsiveness to growth hormone OMIM:[600946], Kowarski syndrome OMIM:[139250], Laron dwarfism OMIM:[600946], Short stature, autosomal dominant, with normal serum growth hormone binding protein OMIM:[600946], Short stature, familial OMIM:[139250], Short stature, idiopathic OMIM:[600946]

About this Structure

1AXI is a Protein complex structure of sequences from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

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 Mon Nov 12 16:03:31 2007