Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein.
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Hydrophobic Matching Controls the Tilt and Stability of the Dimeric Platelet-derived Growth Factor Receptor (PDGFR) Transmembrane SegmentBovine papillomavirus E5 protein induces oligomerization and trans-phosphorylation of the platelet-derived growth factor beta receptor.The bovine papillomavirus E5 protein requires a juxtamembrane negative charge for activation of the platelet-derived growth factor beta receptor and transformation of C127 cells.A single amino acid substitution in a WW-like domain of diverse members of the PDGF receptor subfamily of tyrosine kinases causes constitutive receptor activation.Activation of the erythropoietin receptor by the gp55-P viral envelope protein is determined by a single amino acid in its transmembrane domainThe E5 proteinsMultiple transmembrane amino acid requirements suggest a highly specific interaction between the bovine papillomavirus E5 oncoprotein and the platelet-derived growth factor beta receptor.Viral miniproteinsPapillomavirus E5: the smallest oncoprotein with many functions.Biologically active LIL proteins built with minimal chemical diversity.A single amino acid substitution converts a transmembrane protein activator of the platelet-derived growth factor β receptor into an inhibitor.The bovine papillomavirus E5 protein and the PDGF beta receptor: it takes two to tango.Compensatory mutants of the bovine papillomavirus E5 protein and the platelet-derived growth factor β receptor reveal a complex direct transmembrane interaction.Role of glutamine 17 of the bovine papillomavirus E5 protein in platelet-derived growth factor beta receptor activation and cell transformation.Critical role of the platelet-derived growth factor receptor (PDGFR) beta transmembrane domain in the TEL-PDGFRbeta cytosolic oncoprotein.Productive interaction between transmembrane mutants of the bovine papillomavirus E5 protein and the platelet-derived growth factor beta receptor.In vitro dimerization of the bovine papillomavirus E5 protein transmembrane domain.Two transmembrane dimers of the bovine papillomavirus E5 oncoprotein clamp the PDGF β receptor in an active dimeric conformation.
P2860
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P2860
Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Identification of amino acids ...... ine papillomavirus E5 protein.
@ast
Identification of amino acids ...... ine papillomavirus E5 protein.
@en
type
label
Identification of amino acids ...... ine papillomavirus E5 protein.
@ast
Identification of amino acids ...... ine papillomavirus E5 protein.
@en
prefLabel
Identification of amino acids ...... ine papillomavirus E5 protein.
@ast
Identification of amino acids ...... ine papillomavirus E5 protein.
@en
P2093
P2860
P1433
P1476
Identification of amino acids ...... ine papillomavirus E5 protein.
@en
P2093
P2860
P304
P407
P577
1997-10-01T00:00:00Z