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3bux
From Proteopedia
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|PDB= 3bux |SIZE=350|CAPTION= <scene name='initialview01'>3bux</scene>, resolution 1.350Å | |PDB= 3bux |SIZE=350|CAPTION= <scene name='initialview01'>3bux</scene>, resolution 1.350Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= CBL, CBL2, RNF55 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CBL, CBL2, RNF55 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[3bum|3BUM]], [[3bun|3BUN]], [[3buo|3BUO]], [[3buw|3BUW]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bux OCA], [http://www.ebi.ac.uk/pdbsum/3bux PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bux RCSB]</span> | ||
}} | }} | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:29:14 2008'' |
Revision as of 02:29, 31 March 2008
| |||||||
| , resolution 1.350Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | CBL, CBL2, RNF55 (Homo sapiens) | ||||||
| Related: | 3BUM, 3BUN, 3BUO, 3BUW
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of c-Cbl-TKB domain complexed with its binding motif in c-Met
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.
About this Structure
3BUX 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 Mon Mar 31 05:29:14 2008
Categories: Homo sapiens | Protein complex | Buschdorf, J P. | Guy, G R. | Jackson, R A. | Ng, C. | Sivaraman, J. | Sun, Q. | Atp-binding | Calcium | Cbl | Complex | Cytoplasm | Glycoprotein | Kinase | Ligase | Ligase/signaling protein complex | Membrane | Metal-binding | Nucleotide-binding | Phosphoprotein | Proto-oncogene | Receptor | Sh2 domain | Signal transduction | Tkb | Transferase | Transmembrane | Tyrosine-protein kinase | Ubl conjugation pathway | Zinc | Zinc-finger
