PPIRE14208
Target Protein Information
| Protein_Name | Cerebral cavernous malformations 2 protein |
|---|---|
| Protein_Sequence | MEEEGKKGKKPGIVSPFKRVFLKGEKSRDKKAHEKVTERRPLHTVVLSLPERVEPDRLLSDYIEKEVKYLGQLTSIPGYLNPSSRTEILHFIDNAKRAHQLPGHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAVSYVRDDAAHLVVLKTAQDPGISPSQSLCAESSRGLSAGSLSESAVGPVEACCLVILAAESKVAAEELCCLLGQVFQVVYTESTIDFLDRAIFDGASTPTHHLSLHSDDSSTKVDIKETYEVEASTFCFPESVDVGGASPHSKTISESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFENFLETIGVKDGRGIITDSFGRHRRALSTTSSSTTNGNRATGSSDDRSAPSEGDEWDRMISDISSDIEALGCSMDQDSA |
| Organism_Source | Homo sapiens |
| Functional_Classification | phosphotyrosine-binding domain |
| Cellular_Localization | Cytoplasm |
| Gene_Names | CCM2 |
| UniProt_ID | Q9BSQ5 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | KRIT1Biotin-NPX(Y/F)2-3 |
|---|---|
| Peptide_Sequence | ADTCIYNPLFGSDLQYTNRVDKVVINPYFG |
| Peptide_Length | 30 |
| Peptide_SMILES | CC[C@H](C)[C@H](NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](C)N)[C@@H](C)O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(N)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccccc1)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)NCC(=O)O)[C@@H](C)CC)C(C)C)C(C)C)C(C)C)[C@@H](C)O |
| Chemical_Modification | None |
| Cyclization_Method | None |
| Linear/Cyclic | Linear |
| N-terminal_Modification | Biotinylation |
| C-terminal_Modification | Free |
| Amino_Acid_Distribution | |
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Peptide Physicochemical
| Molecular_Weight | 3423.84 |
|---|---|
| Aliphatic_Index | 84.33333 |
| Aromaticity | 0.16667 |
| Average_Rotatable_Bonds | 3.50000 |
| Charge_at_pH_7 | -1.06550 |
| Isoelectric_Point | 4.31193 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 47 |
| Number_of_Hydrogen_Bond_Donors | 47 |
| Topological_Polar_Surface_Area | 1383.20000 |
| X_logP_energy | -12.37293 |
Interaction Information
| Affinity | KD=14.5 uM |
|---|---|
| Affinity_Assay | Bio-Layer Interferometry |
| PDB_ID | None |
| Type | Affinity ligand |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | Structural basis for the disruption of the cerebral cavernous malformations 2 (CCM2)interaction with Krev interaction trapped 1 (KRIT1)by disease-associated mutations. |
| Release_Year | 2015 |
| PMID | 25525273 |
| DOI | 10.1074/jbc.M114.616433 |