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2d4q

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[[Image:2d4q.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_2d4q| PDB=2d4q | SCENE= }}
{{STRUCTURE_2d4q| PDB=2d4q | SCENE= }}
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'''Crystal structure of the Sec-PH domain of the human neurofibromatosis type 1 protein'''
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===Crystal structure of the Sec-PH domain of the human neurofibromatosis type 1 protein===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_16397625}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16397625 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16397625}}
==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/16397625 16397625]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16397625 16397625]
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Expression, purification and preliminary crystallographic characterization of a novel segment from the neurofibromatosis type 1 protein., Bonneau F, D'Angelo I, Welti S, Stier G, Ylanne J, Scheffzek K, Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2364-7. Epub, 2004 Nov 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15583390 15583390]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Sec14]]
[[Category: Sec14]]
[[Category: Triton x-100]]
[[Category: Triton x-100]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:42:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:43:51 2008''

Revision as of 01:43, 29 July 2008

Image:2d4q.png

Template:STRUCTURE 2d4q

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

Template:ABSTRACT PUBMED 16397625

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

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

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