PPIRE18846
Target Protein Information
| Protein_Name | Adapter molecule crk |
|---|---|
| Protein_Sequence | MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGDQEFDSLPALLEFYKIHYLDTTTLIEPVARSRQGSGVILRQEEAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYRPASASVSALIGGNQEGSHPQPLGGPEPGPYAQPSVNTPLPNLQNGPIYARVIQKRVPNAYDKTALALEVGELVKVTKINVSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS |
| Organism_Source | Mus musculus |
| Functional_Classification | SH3 domain containing proteins |
| Cellular_Localization | Cytoplasm |
| Gene_Names | Crk |
| UniProt_ID | Q64010 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | Sos |
|---|---|
| Peptide_Sequence | PPPVPPRRRR |
| Peptide_Length | 10 |
| Peptide_SMILES | CC(C)[C@H](NC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1)C(=O)N1CCC[C@H]1C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)O |
| Chemical_Modification | None |
| Cyclization_Method | None |
| Linear/Cyclic | Linear |
| N-terminal_Modification | Free |
| C-terminal_Modification | Free |
| Amino_Acid_Distribution | |
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Peptide Physicochemical
| Molecular_Weight | 1227.48 |
|---|---|
| Aliphatic_Index | 29.00000 |
| Aromaticity | 0.00000 |
| Average_Rotatable_Bonds | 3.20000 |
| Charge_at_pH_7 | 3.99797 |
| Isoelectric_Point | 12.97715 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 15 |
| Number_of_Hydrogen_Bond_Donors | 19 |
| Topological_Polar_Surface_Area | 523.67000 |
| X_logP_energy | -5.07992 |
Interaction Information
| Affinity | KD=1.5 uM |
|---|---|
| Affinity_Assay | Isothermal Titration Calorimetry |
| PDB_ID | 1CKB |
| Type | Affinity ligand |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | Role of Electrostatic Interactions in Binding of Peptides and Intrinsically Disordered Proteins to Their Folded Targets. 1. NMR and MD Characterization of the Complex between the c-Crk N-SH3 Domain and the Peptide Sos |
| Release_Year | 2014 |
| PMID | 25207671 |
| DOI | 10.1021/bi500904f |