2d4q

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spinqualitylabelsall models PDB ID 2d4q Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.30Å
Ligands:	,
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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