1luk: Difference between revisions
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[[Image:1luk.jpg|left|200px]]< | [[Image:1luk.jpg|left|200px]] | ||
'''NMR Structure of the Itk SH2 domain, Pro287cis, Energy minimized average structure''' | {{Structure | ||
|PDB= 1luk |SIZE=350|CAPTION= <scene name='initialview01'>1luk</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | |||
|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] | |||
|GENE= | |||
}} | |||
'''NMR Structure of the Itk SH2 domain, Pro287cis, Energy minimized average structure''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LUK is a [ | 1LUK 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=1LUK OCA]. | ||
==Reference== | ==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:[http:// | 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]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:35:22 2008'' | ||
Revision as of 10:35, 20 March 2008
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| Ligands: | ACE and NH2 | ||||||||||||
| 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, Pro287cis, Energy minimized average structure
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
1LUK 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
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