Structural Plasticity in Remodeled Protein-Protein Interface
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 apentamutant of hGH by phage display that fills the cavity and l...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1997-11, Vol.278 (5340), p.1125-1128 |
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| creator | Atwell, Shane Ultsch, Mark De Vos, Abraham M. Wells, James A. |
| description | 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 apentamutant of hGH by phage display that fills the cavity and largely restores binding affinity. A 2.1 $\angst $ 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. |
| doi_str_mv | 10.1126/science.278.5340.1125 |
| format | Article |
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A 2.1 $\angst $ 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. 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Psychology ; Hormone receptors ; Hormones ; Human Growth Hormone - chemistry ; Human Growth Hormone - genetics ; Human Growth Hormone - metabolism ; Humans ; Hydrogen Bonding ; Hydrogen bonds ; Libraries ; Models, Molecular ; Mutagenesis ; Mutation ; Peptide Library ; Physiological aspects ; Protein Binding ; Protein Conformation ; Proteins ; Receptors ; Renovations ; Somatotropin ; Somatotropin receptors</subject><ispartof>Science (American Association for the Advancement of Science), 1997-11, Vol.278 (5340), p.1125-1128</ispartof><rights>Copyright 1997 American Association for the Advancement of Science</rights><rights>1998 INIST-CNRS</rights><rights>COPYRIGHT 1997 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1997 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Nov 7, 1997</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c785t-38d86803cac2c662ca326dfdf25cdd8312f62054bbe8302dee51119961ba11423</citedby><cites>FETCH-LOGICAL-c785t-38d86803cac2c662ca326dfdf25cdd8312f62054bbe8302dee51119961ba11423</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2894253$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2894253$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2870,2871,27903,27904,57995,58228</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2057630$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9353194$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Atwell, Shane</creatorcontrib><creatorcontrib>Ultsch, Mark</creatorcontrib><creatorcontrib>De Vos, Abraham M.</creatorcontrib><creatorcontrib>Wells, James A.</creatorcontrib><title>Structural Plasticity in Remodeled Protein-Protein Interface</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>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 apentamutant of hGH by phage display that fills the cavity and largely restores binding affinity. 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A 2.1 $\angst $ 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.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>9353194</pmid><doi>10.1126/science.278.5340.1125</doi><tpages>4</tpages></addata></record> |
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| ispartof | Science (American Association for the Advancement of Science), 1997-11, Vol.278 (5340), p.1125-1128 |
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| language | eng |
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| source | MEDLINE; American Association for the Advancement of Science; Jstor Complete Legacy |
| subjects | Analytical, structural and metabolic biochemistry Atoms Bacteriophages Binding and carrier proteins Biochemistry Biological and medical sciences Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Colors Crystallography, X-Ray Data collection Fundamental and applied biological sciences. Psychology Hormone receptors Hormones Human Growth Hormone - chemistry Human Growth Hormone - genetics Human Growth Hormone - metabolism Humans Hydrogen Bonding Hydrogen bonds Libraries Models, Molecular Mutagenesis Mutation Peptide Library Physiological aspects Protein Binding Protein Conformation Proteins Receptors Renovations Somatotropin Somatotropin receptors |
| title | Structural Plasticity in Remodeled Protein-Protein Interface |
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