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Cited by 180

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Structural Plasticity in a Remodeled Protein-Protein Interface

Atwell, Shane, Ultsch, Mark, De Vos, Abraham M., Wells, James A.·1997·Science

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 Å 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.

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Crossref · 10.1126/science.278.5340.1125

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Metadata

Authors
Atwell, S., Ultsch, M., De Vos, A. M., & Wells, J. A.
Venue
Science
Published
1997-11-07
Volume
278
Issue
5340
Pages
1125-1128
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2086518221
Cited by
180
References
1
FWCI
4.50
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Structural Plasticity in a Remodeled Protein-Protein Interface. https://app.cochat.ai/papers/10.1126/science.278.5340.1125
The paper
Atwell, S., Ultsch, M., De Vos, A. M., & Wells, J. A. (1997). Structural Plasticity in a Remodeled Protein-Protein Interface. Science. https://doi.org/10.1126/science.278.5340.1125

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.