This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3buo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3buo.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3buo.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3buo| PDB=3buo | SCENE= }}
{{STRUCTURE_3buo| PDB=3buo | SCENE= }}
-
'''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==
+
<!--
-
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
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18273061 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18273061}}
==About this Structure==
==About this Structure==
Line 59: Line 63:
[[Category: Zinc]]
[[Category: Zinc]]
[[Category: Zinc-finger]]
[[Category: Zinc-finger]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:07:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:36:26 2008''

Revision as of 10:36, 27 July 2008

Image:3buo.png

Template:STRUCTURE 3buo

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

Template:ABSTRACT PUBMED 18273061

About this Structure

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

Reference

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

Page seeded by OCA on Sun Jul 27 13:36:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3buo"
Personal tools