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Structure paper

TitleStructural and biochemical consequences of NF1 associated nontruncating mutations in the Sec14-PH module of neurofibromin.
Journal, issue, pagesHum. Mutat., Vol. 32, Page 191-197, Year 2011
Publish dateOct 13, 2010 (structure data deposition date)
AuthorsWelti, S. / Kuhn, S. / D'Angelo, I. / Brugger, B. / Kaufmann, D. / Scheffzek, K.
External linksHum. Mutat. / PubMed:21089070
MethodsX-ray diffraction
Resolution2.189 - 2.65 Å
Structure data

PDB-3p7z:
Crystal structure of the Neurofibromin Sec14-PH module containing the patient derived mutation I1584V
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-3peg:
Crystal structure of Neurofibromins Sec14-PH module containing a patient derived duplication (TD)
Method: X-RAY DIFFRACTION / Resolution: 2.524 Å

PDB-3pg7:
Crystal structure of the H. sapiens NF1 SEC-PH domain (del1750 mutant)
Method: X-RAY DIFFRACTION / Resolution: 2.189 Å

Chemicals

ChemComp-PEV:
(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / POPE, phospholipid*YM

ChemComp-NA:
Unknown entry

ChemComp-POP:
PYROPHOSPHATE 2-

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-MG:
Unknown entry

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

Source
  • homo sapiens (human)
KeywordsLIPID BINDING PROTEIN / Sec14 homolgy domain / pleckstrin homology domain / binding of glycerophospholipids / glycerophospholipids / cytoplasmatic / Sec14 domain / PH domain / Phosphatidylethanolamin Binding / Lipid Binding / SEC lipid binding domain

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