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2d4q

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2d4q, resolution 2.30Å ()

Ligands:

Gene:

neurofibromin (Homo sapiens)

Domains:

SEC14

Structural annotation:
Resources:	InterPro : Ipr001936, Ipr008936, Ipr001251 UniProt : P21359

Functional annotation:
Resources:	GeneCard : NF1
Cellular component:	axon dendrite intracellular cytoplasm nucleus
Biological process:	regulation of bone resorption negative regulation of cell cycle negative regulation of oligodendrocyte differentiation Schwann cell development cognition positive regulation of Ras GTPase activity negative regulation of neuroblast proliferation regulation of glial cell differentiation brain development smooth muscle development pigmentation liver development MAPKKK cascade adrenal gland development camera-type eye morphogenesis negative regulation of MAPKKK cascade positive regulation of apoptosis cell communication negative regulation of protein kinase activity heart development regulation of angiogenesis actin cytoskeleton organization and biogenesis artery morphogenesis negative regulation of MAP kinase activity regulation of Ras GTPase activity negative regulation of cell migration regulation of cell-matrix adhesion wound healing cerebral cortex development regulation of small GTPase mediated signal transduction cell cycle positive regulation of neuron apoptosis visual learning myelination in the peripheral nervous system negative regulation of endothelial cell proliferation metanephros development positive regulation of adenylate cyclase activity peripheral nervous system development spinal cord development forebrain morphogenesis forebrain astrocyte development phosphoinositide 3-kinase cascade Ras protein signal transduction osteoblast differentiation sympathetic nervous system development negative regulation of transcription factor import into nucleus response to hypoxia extracellular matrix organization and biogenesis regulation of blood vessel endothelial cell migration collagen fibril organization
Molecular function:	GTPase activator activity protein binding Ras GTPase activator activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

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

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2D4Q is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

D'Angelo I, Welti S, Bonneau F, Scheffzek K. A novel bipartite phospholipid-binding module in the neurofibromatosis type 1 protein. EMBO Rep. 2006 Feb;7(2):174-9. PMID:16397625
Bonneau F, D'Angelo I, Welti S, Stier G, Ylanne J, Scheffzek K. Expression, purification and preliminary crystallographic characterization of a novel segment from the neurofibromatosis type 1 protein. Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2364-7. Epub, 2004 Nov 26. PMID:15583390

Page seeded by OCA on Tue Feb 17 20:46:22 2009

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2d4q

From Proteopedia

Crystal structure of the Sec-PH domain of the human neurofibromatosis type 1 protein

About this Structure

Reference

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