2d4q: Difference between revisions
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|PDB= 2d4q |SIZE=350|CAPTION= <scene name='initialview01'>2d4q</scene>, resolution 2.30Å | |PDB= 2d4q |SIZE=350|CAPTION= <scene name='initialview01'>2d4q</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=OXN:OXTOXYNOL-10'>OXN</scene> | |LIGAND= <scene name='pdbligand=OXN:OXTOXYNOL-10'>OXN</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= neurofibromin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= neurofibromin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d4q OCA], [http://www.ebi.ac.uk/pdbsum/2d4q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d4q RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
Neurofibromatosis type 1 (NF1) is a common tumour predisposition syndrome associated with numerous clinical complications. Mutations in the tumour suppressor gene NF1 are responsible for disease pathogenesis. This gene encodes the 320 kDa protein neurofibromin, the only clearly defined function of which is to act as a Ras-specific GTPase-activating protein (RasGAP). Here we report the structural discovery of a novel module in neurofibromin, composed of a Sec14p homologous segment and a previously undetected pleckstrin homology (PH)-like domain of potentially novel function. We show phospholipid binding by this bipartite module and identify residues that are involved in this activity; we also show that the PH-like domain is not sufficient for lipid binding. The unique architecture of the domain interface points to a model of how the PH-like domain may regulate binding of a ligand by the Sec14 module. | Neurofibromatosis type 1 (NF1) is a common tumour predisposition syndrome associated with numerous clinical complications. Mutations in the tumour suppressor gene NF1 are responsible for disease pathogenesis. This gene encodes the 320 kDa protein neurofibromin, the only clearly defined function of which is to act as a Ras-specific GTPase-activating protein (RasGAP). Here we report the structural discovery of a novel module in neurofibromin, composed of a Sec14p homologous segment and a previously undetected pleckstrin homology (PH)-like domain of potentially novel function. We show phospholipid binding by this bipartite module and identify residues that are involved in this activity; we also show that the PH-like domain is not sufficient for lipid binding. The unique architecture of the domain interface points to a model of how the PH-like domain may regulate binding of a ligand by the Sec14 module. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Welti, S.]] | [[Category: Welti, S.]] | ||
[[Category: angelo, I D.]] | [[Category: angelo, I D.]] | ||
[[Category: beta hairpin]] | [[Category: beta hairpin]] | ||
[[Category: cral_trio]] | [[Category: cral_trio]] | ||
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[[Category: triton x-100]] | [[Category: triton x-100]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:30:25 2008'' | ||
Revision as of 23:30, 30 March 2008
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| 2d4q, resolution 2.30Å | |||||||||||||
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| Ligands: | OXN, POP | ||||||||||||
| Gene: | neurofibromin (Homo sapiens) | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of the Sec-PH domain of the human neurofibromatosis type 1 protein
Overview
Neurofibromatosis type 1 (NF1) is a common tumour predisposition syndrome associated with numerous clinical complications. Mutations in the tumour suppressor gene NF1 are responsible for disease pathogenesis. This gene encodes the 320 kDa protein neurofibromin, the only clearly defined function of which is to act as a Ras-specific GTPase-activating protein (RasGAP). Here we report the structural discovery of a novel module in neurofibromin, composed of a Sec14p homologous segment and a previously undetected pleckstrin homology (PH)-like domain of potentially novel function. We show phospholipid binding by this bipartite module and identify residues that are involved in this activity; we also show that the PH-like domain is not sufficient for lipid binding. The unique architecture of the domain interface points to a model of how the PH-like domain may regulate binding of a ligand by the Sec14 module.
About this Structure
2D4Q is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A novel bipartite phospholipid-binding module in the neurofibromatosis type 1 protein., D'Angelo I, Welti S, Bonneau F, Scheffzek K, EMBO Rep. 2006 Feb;7(2):174-9. PMID:16397625
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