1p8t

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(New page: 200px<br /> <applet load="1p8t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p8t, resolution 3.2&Aring;" /> '''Crystal structure of...)
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<applet load="1p8t" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1p8t, resolution 3.2&Aring;" />
'''Crystal structure of Nogo-66 Receptor'''<br />
'''Crystal structure of Nogo-66 Receptor'''<br />
==Overview==
==Overview==
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The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration, after injury of the spinal cord and brain. These cell-surface proteins, signal through multi-subunit neuronal receptors that contain a common, ligand-binding glycosylphosphatidylinositol-anchored subunit termed the, Nogo-66 receptor (NgR). By deletion analysis, we show that the binding of, soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the, entire leucine-rich repeat (LRR) region of NgR, but not other portions of, the protein. Despite sharing extensive sequence similarity with NgR, two, related proteins, NgR2 and NgR3, which we have identified, do not bind, Nogo, MAG, OMgp or NgR. To investigate NgR specificity and multi-ligand, binding, we determined the crystal structure of the biologically active, ligand-binding soluble ectodomain of NgR. The molecule is banana shaped, with elongation and curvature arising from eight LRRs flanked by an, N-terminal cap and a small C-terminal subdomain. The NgR structure, analysis, as well as a comparison of NgR surface residues not conserved in, NgR2 and NgR3, identifies potential protein interaction sites important in, the assembly of a functional signaling complex.
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The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain. These cell-surface proteins signal through multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR). By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein. Despite sharing extensive sequence similarity with NgR, two related proteins, NgR2 and NgR3, which we have identified, do not bind Nogo, MAG, OMgp or NgR. To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR. The molecule is banana shaped with elongation and curvature arising from eight LRRs flanked by an N-terminal cap and a small C-terminal subdomain. The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1P8T 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 NAG and NDG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P8T OCA].
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1P8T 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=NAG:'>NAG</scene> and <scene name='pdbligand=NDG:'>NDG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P8T OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Barton, W.A.]]
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[[Category: Barton, W A.]]
[[Category: Cate, R.]]
[[Category: Cate, R.]]
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[[Category: Fournier, A.E.]]
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[[Category: Fournier, A E.]]
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[[Category: Jeffrey, P.D.]]
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[[Category: Jeffrey, P D.]]
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[[Category: Liu, B.P.]]
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[[Category: Liu, B P.]]
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[[Category: Nikolov, D.B.]]
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[[Category: Nikolov, D B.]]
[[Category: Sah, D.]]
[[Category: Sah, D.]]
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[[Category: Strittmatter, S.M.]]
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[[Category: Strittmatter, S M.]]
[[Category: Tzvetkova, D.]]
[[Category: Tzvetkova, D.]]
[[Category: NAG]]
[[Category: NAG]]
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[[Category: nogo-66]]
[[Category: nogo-66]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:40:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:22 2008''

Revision as of 12:26, 21 February 2008


1p8t, resolution 3.2Å

Drag the structure with the mouse to rotate

Crystal structure of Nogo-66 Receptor

Contents

Overview

The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain. These cell-surface proteins signal through multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR). By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein. Despite sharing extensive sequence similarity with NgR, two related proteins, NgR2 and NgR3, which we have identified, do not bind Nogo, MAG, OMgp or NgR. To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR. The molecule is banana shaped with elongation and curvature arising from eight LRRs flanked by an N-terminal cap and a small C-terminal subdomain. The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.

Disease

Known diseases associated with this structure: Schizophrenia, susceptibility to OMIM:[605566]

About this Structure

1P8T is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins., Barton WA, Liu BP, Tzvetkova D, Jeffrey PD, Fournier AE, Sah D, Cate R, Strittmatter SM, Nikolov DB, EMBO J. 2003 Jul 1;22(13):3291-302. PMID:12839991

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