PPIRE02989
Target Protein Information
| Protein_Name | H-2 class I histocompatibility antigen, K-Q alpha chain |
|---|---|
| Protein_Sequence | PRFISVGYVDDTELVRFDSDAENPRYEPRARWMEQVEPEYWERNTQIAKDNEQSSRVDLRTLLRYYNQSAGGSHTIQRMYGCDVGSDGRLLRGYEQVAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGAAERRRAYLEGACVEWLSRHLKNGNATLLRTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPKPLTLRWEPPPSAVSNTVIIAVLVVLGAAIVTGAVVAFVMMRRRNTGGKGGDYALAPGSQTSDLSLPDCKVMVHDPHSLA |
| Organism_Source | Mus musculus |
| Functional_Classification | Immune-related protein |
| Cellular_Localization | Plasma membrane |
| Gene_Names | H2-K1 |
| UniProt_ID | P14428 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | VSV8 |
|---|---|
| Peptide_Sequence | RGYVYQGL |
| Peptide_Length | 8 |
| Peptide_SMILES | CC(C)C[C@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@@H](NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)CNC(=O)[C@@H](N)CCCNC(=N)N)C(C)C)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 | 955.08 |
|---|---|
| Aliphatic_Index | 85.00000 |
| Aromaticity | 0.25000 |
| Average_Rotatable_Bonds | 3.62500 |
| Charge_at_pH_7 | 0.99628 |
| Isoelectric_Point | 9.17163 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 13 |
| Number_of_Hydrogen_Bond_Donors | 15 |
| Topological_Polar_Surface_Area | 412.47000 |
| X_logP_energy | -2.81783 |
Interaction Information
| Affinity | KD=20 nM |
|---|---|
| Affinity_Assay | NMR chemical shift perturbation |
| PDB_ID | None |
| Type | Affinity ligand |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | The crystal structures of K(bm1)and K(bm8)reveal that subtle changes in the peptide environment impact thermostability and alloreactivity. |
| Release_Year | 2001 |
| PMID | 11290333 |
| DOI | 10.1016/s1074-7613(01)00105-4 |