3bun: Difference between revisions
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|PDB= 3bun |SIZE=350|CAPTION= <scene name='initialview01'>3bun</scene>, resolution 2.000Å | |PDB= 3bun |SIZE=350|CAPTION= <scene name='initialview01'>3bun</scene>, resolution 2.000Å | ||
|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]], [[3buo|3BUO]], [[3buw|3BUW]], [[3bux|3BUX]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bun OCA], [http://www.ebi.ac.uk/pdbsum/3bun PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bun 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 05:29:10 2008'' | ||
Revision as of 05:29, 31 March 2008
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| , resolution 2.000Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | CBL, CBL2, RNF55 (Homo sapiens) | ||||||
| Related: | 3BUM, 3BUO, 3BUW, 3BUX
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of c-Cbl-TKB domain complexed with its binding motif in Sprouty4
OverviewOverview
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 StructureAbout this Structure
3BUN 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- Pages with broken file links
- Homo sapiens
- Protein complex
- Buschdorf, J P.
- Guy, G R.
- Jackson, R A.
- Ng, C.
- Sivaraman, J.
- Sun, Q.
- Alternative splicing
- Calcium
- Cbl
- Complex
- Cytoplasm
- Developmental protein
- Ligase
- Ligase/signaling protein complex
- Membrane
- Metal-binding
- Phosphoprotein
- Proto-oncogene
- Sh2 domain
- Signal transduction
- Tkb
- Ubl conjugation pathway
- Zinc
- Zinc-finger