2d4q

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(New page: 200px<br /> <applet load="2d4q" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d4q, resolution 2.30&Aring;" /> '''Crystal structure o...)
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[[Image:2d4q.gif|left|200px]]<br />
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[[Image:2d4q.gif|left|200px]]<br /><applet load="2d4q" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2d4q" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2d4q, resolution 2.30&Aring;" />
caption="2d4q, resolution 2.30&Aring;" />
'''Crystal structure of the Sec-PH domain of the human neurofibromatosis type 1 protein'''<br />
'''Crystal structure of the Sec-PH domain of the human neurofibromatosis type 1 protein'''<br />
==Overview==
==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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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.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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2D4Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with OXN and POP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D4Q OCA].
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2D4Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=OXN:'>OXN</scene> and <scene name='pdbligand=POP:'>POP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D4Q OCA].
==Reference==
==Reference==
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[[Category: Scheffzek, K.]]
[[Category: Scheffzek, K.]]
[[Category: Welti, S.]]
[[Category: Welti, S.]]
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[[Category: angelo, I.D.]]
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[[Category: angelo, I D.]]
[[Category: OXN]]
[[Category: OXN]]
[[Category: POP]]
[[Category: POP]]
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[[Category: triton x-100]]
[[Category: triton x-100]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:26:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:22 2008''

Revision as of 14:55, 21 February 2008

Image:2d4q.gif

2d4q, resolution 2.30Å

Drag the structure with the mouse to rotate

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

Contents

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.

Disease

Known diseases associated with this structure: Leukemia, juvenile myelomonocytic OMIM:[162200], Melanoma, desmoplastic neurotropic OMIM:[162200], Neurofibromatosis, familial spinal OMIM:[162200], Neurofibromatosis, type 1 OMIM:[162200], Neurofibromatosis-Noonan syndrome OMIM:[162200], Pseudarthrosis, tibial, in NF1 OMIM:[162200], Watson syndrome OMIM:[162200]

About this Structure

2D4Q is a Single protein structure of sequence from Homo sapiens with and as ligands. 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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