1lum

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(New page: 200px<br /><applet load="1lum" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lum" /> '''NMR Structure of the Itk SH2 domain, Pro287t...)
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'''NMR Structure of the Itk SH2 domain, Pro287trans, 20 low energy structures'''<br />
'''NMR Structure of the Itk SH2 domain, Pro287trans, 20 low energy structures'''<br />
==Overview==
==Overview==
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Interleukin-2 tyrosine kinase (Itk) is a T cell-specific kinase required, for a proper immune response following T cell receptor engagement. In, addition to the kinase domain, Itk is composed of several noncatalytic, regulatory domains, including a Src homology 2 (SH2) domain that contains, a conformationally heterogeneous Pro residue. Cis-trans isomerization of a, single prolyl imide bond within the SH2 domain mediates conformer-specific, ligand recognition that may have functional implications in T cell, signaling. To better understand the mechanism by which a proline switch, regulates ligand binding, we have used NMR spectroscopy to determine two, structures of Itk SH2 corresponding to the cis and trans imide, bond-containing conformers. The structures indicate that the heterogeneous, Pro residue acts as a hinge that modulates ligand recognition by, controlling the relative orientation of protein-binding surfaces.
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Interleukin-2 tyrosine kinase (Itk) is a T cell-specific kinase required for a proper immune response following T cell receptor engagement. In addition to the kinase domain, Itk is composed of several noncatalytic regulatory domains, including a Src homology 2 (SH2) domain that contains a conformationally heterogeneous Pro residue. Cis-trans isomerization of a single prolyl imide bond within the SH2 domain mediates conformer-specific ligand recognition that may have functional implications in T cell signaling. To better understand the mechanism by which a proline switch regulates ligand binding, we have used NMR spectroscopy to determine two structures of Itk SH2 corresponding to the cis and trans imide bond-containing conformers. The structures indicate that the heterogeneous Pro residue acts as a hinge that modulates ligand recognition by controlling the relative orientation of protein-binding surfaces.
==About this Structure==
==About this Structure==
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1LUM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LUM OCA].
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1LUM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LUM OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Transferase]]
[[Category: Transferase]]
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[[Category: Andreotti, A.H.]]
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[[Category: Andreotti, A H.]]
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[[Category: Brazin, K.N.]]
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[[Category: Brazin, K N.]]
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[[Category: Fulton, D.B.]]
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[[Category: Fulton, D B.]]
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[[Category: Mallis, R.J.]]
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[[Category: Mallis, R J.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: NH2]]
[[Category: NH2]]
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[[Category: tsk]]
[[Category: tsk]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:54:11 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:36 2008''

Revision as of 11:48, 21 February 2008


1lum

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NMR Structure of the Itk SH2 domain, Pro287trans, 20 low energy structures

Overview

Interleukin-2 tyrosine kinase (Itk) is a T cell-specific kinase required for a proper immune response following T cell receptor engagement. In addition to the kinase domain, Itk is composed of several noncatalytic regulatory domains, including a Src homology 2 (SH2) domain that contains a conformationally heterogeneous Pro residue. Cis-trans isomerization of a single prolyl imide bond within the SH2 domain mediates conformer-specific ligand recognition that may have functional implications in T cell signaling. To better understand the mechanism by which a proline switch regulates ligand binding, we have used NMR spectroscopy to determine two structures of Itk SH2 corresponding to the cis and trans imide bond-containing conformers. The structures indicate that the heterogeneous Pro residue acts as a hinge that modulates ligand recognition by controlling the relative orientation of protein-binding surfaces.

About this Structure

1LUM is a Single protein structure of sequence from Mus musculus with and as ligands. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.

Reference

Structural characterization of a proline-driven conformational switch within the Itk SH2 domain., Mallis RJ, Brazin KN, Fulton DB, Andreotti AH, Nat Struct Biol. 2002 Dec;9(12):900-5. PMID:12402030

Page seeded by OCA on Thu Feb 21 13:48:36 2008

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