1k2p: Difference between revisions
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[[Image:1k2p.jpg|left|200px]] | [[Image:1k2p.jpg|left|200px]] | ||
'''Crystal structure of Bruton's tyrosine kinase domain''' | {{Structure | ||
|PDB= 1k2p |SIZE=350|CAPTION= <scene name='initialview01'>1k2p</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= | |||
|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= | |||
}} | |||
'''Crystal structure of Bruton's tyrosine kinase domain''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1K2P is a [ | 1K2P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K2P OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of Bruton's tyrosine kinase domain suggests a novel pathway for activation and provides insights into the molecular basis of X-linked agammaglobulinemia., Mao C, Zhou M, Uckun FM, J Biol Chem. 2001 Nov 2;276(44):41435-43. Epub 2001 Aug 29. PMID:[http:// | Crystal structure of Bruton's tyrosine kinase domain suggests a novel pathway for activation and provides insights into the molecular basis of X-linked agammaglobulinemia., Mao C, Zhou M, Uckun FM, J Biol Chem. 2001 Nov 2;276(44):41435-43. Epub 2001 Aug 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11527964 11527964] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: kinase domain]] | [[Category: kinase domain]] | ||
''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 12:11:46 2008'' | ||
Revision as of 13:11, 20 March 2008
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| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 | ||||||
Crystal structure of Bruton's tyrosine kinase domain
OverviewOverview
Bruton's tyrosine kinase is intimately involved in signal transduction pathways regulating survival, activation, proliferation, and differentiation of B lineage lymphoid cells. Mutations in the human btk gene are the cause of X-linked agammaglobulinemia, a male immune deficiency disorder characterized by a lack of mature, immunoglobulin-producing B lymphocytes. We have determined the x-ray crystal structure of the Bruton's tyrosine kinase kinase domain in its unphosphorylated state to a 2.1 A resolution. A comparison with the structures of other tyrosine kinases and a possible mechanism of activation unique to Bruton's tyrosine kinase are provided.
DiseaseDisease
Known diseases associated with this structure: Agammaglobulinemia, type 1, X-linked OMIM:[300300], XLA and isolated growth hormone deficiency OMIM:[300300]
About this StructureAbout this Structure
1K2P is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Bruton's tyrosine kinase domain suggests a novel pathway for activation and provides insights into the molecular basis of X-linked agammaglobulinemia., Mao C, Zhou M, Uckun FM, J Biol Chem. 2001 Nov 2;276(44):41435-43. Epub 2001 Aug 29. PMID:11527964
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