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PDB: 4 results

3I2T
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BU of 3i2t by Molmil
Crystal structure of the unliganded Drosophila Epidermal Growth Factor Receptor ectodomain
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, Epidermal growth factor receptor, ...
Authors:Alvarado, D, Klein, D.E, Lemmon, M.A.
Deposit date:2009-06-29
Release date:2009-09-08
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (2.7 Å)
Cite:ErbB2 resembles an autoinhibited invertebrate epidermal growth factor receptor.
Nature, 461, 2009
3LTF
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BU of 3ltf by Molmil
Crystal Structure of the Drosophila Epidermal Growth Factor Receptor ectodomain in complex with Spitz
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, Epidermal growth factor receptor, ...
Authors:Alvarado, D, Klein, D.E, Lemmon, M.A.
Deposit date:2010-02-15
Release date:2010-08-25
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (3.2 Å)
Cite:Structural basis for negative cooperativity in growth factor binding to an EGF receptor.
Cell(Cambridge,Mass.), 142, 2010
3LTG
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BU of 3ltg by Molmil
Crystal structure of the Drosophila Epidermal Growth Factor Receptor ectodomain complexed with a low affinity Spitz mutant
Descriptor: Epidermal growth factor receptor, Protein spitz
Authors:Alvarado, D, Klein, D.E, Lemmon, M.A.
Deposit date:2010-02-15
Release date:2010-08-25
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (3.4 Å)
Cite:Structural basis for negative cooperativity in growth factor binding to an EGF receptor.
Cell(Cambridge,Mass.), 142, 2010
3GOP
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BU of 3gop by Molmil
Crystal structure of the EGF receptor juxtamembrane and kinase domains
Descriptor: Epidermal growth factor receptor
Authors:Choi, S.H, Alvarado, D, Moravcevic, K, Lemmon, M.A.
Deposit date:2009-03-19
Release date:2009-07-07
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:The juxtamembrane region of the EGF receptor functions as an activation domain.
Mol.Cell, 34, 2009

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