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1lum

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[[Image:1lum.jpg|left|200px]]<br /><applet load="1lum" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lum.jpg|left|200px]]
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caption="1lum" />
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'''NMR Structure of the Itk SH2 domain, Pro287trans, 20 low energy structures'''<br />
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{{Structure
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|PDB= 1lum |SIZE=350|CAPTION= <scene name='initialview01'>1lum</scene>
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|SITE=
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|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''NMR Structure of the Itk SH2 domain, Pro287trans, 20 low energy structures'''
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==Overview==
==Overview==
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==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 <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].
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1LUM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LUM OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12402030 12402030]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12402030 12402030]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: tsk]]
[[Category: tsk]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:35:27 2008''

Revision as of 10:35, 20 March 2008


PDB ID 1lum

Drag the structure with the mouse to rotate
Ligands: and
Activity: Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2
Coordinates: save as pdb, mmCIF, xml



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. 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 Mar 20 12:35:27 2008

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