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Structure paper

TitleStructural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations.
Journal, issue, pagesSci. Signal., Vol. 7, Page ra114-ra114, Year 2014
Publish dateOct 7, 2014 (structure data deposition date)
AuthorsLittlefield, P. / Liu, L. / Mysore, V. / Shan, Y. / Shaw, D.E. / Jura, N.
External linksSci. Signal. / PubMed:25468994
MethodsX-ray diffraction
Resolution2.981 - 3.1 Å
Structure data

PDB-4riw:
Crystal structure of an EGFR/HER3 kinase domain heterodimer
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-4rix:
Crystal structure of an EGFR/HER3 kinase domain heterodimer containing the cancer-associated HER3-Q790R mutation
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-4riy:
Crystal structure of an EGFR/HER3 kinase domain heterodimer containing the cancer-associated HER3-E909G mutation
Method: X-RAY DIFFRACTION / Resolution: 2.981 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / RECEPTOR TYROSINE KINASE / PSEUDOKINASE / KINASE / ATP BINDING / MEMBRANE

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