2fci: Difference between revisions
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New page: left|200px<br /><applet load="2fci" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fci" /> '''Structural basis for the requirement of two ... |
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[[Image:2fci.gif|left|200px]]<br /><applet load="2fci" size=" | [[Image:2fci.gif|left|200px]]<br /><applet load="2fci" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2fci" /> | caption="2fci" /> | ||
'''Structural basis for the requirement of two phosphotyrosines in signaling mediated by Syk tyrosine kinase'''<br /> | '''Structural basis for the requirement of two phosphotyrosines in signaling mediated by Syk tyrosine kinase'''<br /> | ||
==Overview== | ==Overview== | ||
The protein-tyrosine kinase Syk couples immune recognition receptors to | The protein-tyrosine kinase Syk couples immune recognition receptors to multiple signal transduction pathways, including the mobilization of calcium and the activation of NFAT. The ability of Syk to regulate signaling is influenced by its phosphorylation on tyrosine residues within the linker B region. The phosphorylation of both Y342 and Y346 is necessary for optimal signaling from the B cell receptor for antigen. The SH2 domains of multiple signaling proteins share the ability to bind this doubly phosphorylated site. The NMR structure of the C-terminal SH2 domain of PLCgamma (PLCC) bound to a doubly phosphorylated Syk peptide reveals a novel mode of phosphotyrosine recognition. PLCC undergoes extensive conformational changes upon binding to form a second phosphotyrosine-binding pocket in which pY346 is largely desolvated and stabilized through electrostatic interactions. The formation of the second binding pocket is distinct from other modes of phosphotyrosine recognition in SH2-protein association. The dependence of signaling on simultaneous phosphorylation of these two tyrosine residues offers a new mechanism to fine-tune the cellular response to external stimulation. | ||
==About this Structure== | ==About this Structure== | ||
2FCI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | 2FCI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2FCI OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Geahlen, R | [[Category: Geahlen, R L.]] | ||
[[Category: Groesch, T | [[Category: Groesch, T D.]] | ||
[[Category: Mattila, S.]] | [[Category: Mattila, S.]] | ||
[[Category: Post, C | [[Category: Post, C B.]] | ||
[[Category: Zhou, F.]] | [[Category: Zhou, F.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
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[[Category: syk kinase]] | [[Category: syk kinase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:01 2008'' | ||
