3buo: Difference between revisions

Revision as of 13:36, 27 July 2008

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File:3buo.png

Template:STRUCTURE 3buo

Crystal structure of c-Cbl-TKB domain complexed with its binding motif in EGF receptor'Crystal structure of c-Cbl-TKB domain complexed with its binding motif in EGF receptor'

Template:ABSTRACT PUBMED 18273061

About this StructureAbout this Structure

3BUO is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for a novel intrapeptidyl H-bond and reverse binding of c-Cbl-TKB domain substrates., Ng C, Jackson RA, Buschdorf JP, Sun Q, Guy GR, Sivaraman J, EMBO J. 2008 Feb 14;. PMID:18273061

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of c-Cbl-TKB domain complexed with its binding motif in EGF receptor''''
+===Crystal structure of c-Cbl-TKB domain complexed with its binding motif in EGF receptor'===
-==Overview==
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-The c-Cbl tyrosine kinase binding domain (Cbl-TKB), essentially an 'embedded' SH2 domain, has a critical role in targeting proteins for ubiquitination. To address how this domain can bind to disparate recognition mofits and to determine whether this results in variations in substrate-binding affinity, we compared crystal structures of the Cbl-TKB domain complexed with phosphorylated peptides of Sprouty2, Sprouty4, epidermal growth factor receptor, Syk, and c-Met receptors and validated the binding with point-mutational analyses using full-length proteins. An obligatory, intrapeptidyl H-bond between the phosphotyrosine and the conserved asparagine or adjacent arginine is essential for binding and orientates the peptide into a positively charged pocket on c-Cbl. Surprisingly, c-Met bound to Cbl in the reverse direction, which is unprecedented for SH2 domain binding. The necessity of this intrapeptidyl H-bond was confirmed with isothermal titration calorimetry experiments that also showed Sprouty2 to have the highest binding affinity to c-Cbl; this may enable the selective sequestration of c-Cbl from other target proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_18273061}}, adds the Publication Abstract to the page
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