PPIRE14596

Target Protein Information
Protein_Name Calcitonin gene-related peptide type 1 receptor
Protein_Sequence MDKKHILCFLVLLPLNMALISAESEEGVNQTDLGVTRNKIMTAQYECYQKIMQDPIQQAEGLYCNRTWDGWLCWNDVAAGTESMQYCPDYFQDFDPSEKVTKICDQDGHWFRHPDSNRTWTNYTLCNNSTHEKVKTALNLFYLTIIGHGLSIASLIISLIIFFYFKSLSCQRITLHKNLFFSFICNSIVTIIHLTAVANNQALVATNPVSCKVSQFIHLYLMGCNYFWMLCEGVYLHTLIVVAVFAEKQHLMWYYFLGWGFPLLPACIHAIARSLYYNDNCWISSDTHLLYIIHGPICAALLVNLFFLLNIVRVLITKLKVTHQVESNLYMKAVRATLILVPLLGIEFVLFPWRPEGKVAEEVYDYVMHILMHFQGLLVATIFCFFNGEVQAILRRNWNQYKIQFGNGFSHSDALRSASYTVSTISDMQGYSHDCPTEHLNGKSIQDIENVALKSENMYDLVM
Organism_Source Mus musculus
Functional_Classification G protein-coupled receptor
Cellular_Localization Plasma membrane
Gene_Names Calcrl
UniProt_ID Q9R1W5
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name human calcitonin gene-related peptide(CGRP)
Peptide_Sequence AHSDGTFTSDYSKYLDSRRAQDFVQWLMNTLGKALSG
Peptide_Length 37
Peptide_SMILES CSCC[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](C)N)[C@@H](C)O)[C@@H](C)O)C(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)NCC(=O)O)[C@@H](C)O
Chemical_Modification None
Cyclization_Method Side chain-side chain cyclization; C2<->C7; disulfide bond
Linear/Cyclic Cyclic
N-terminal_Modification Free
C-terminal_Modification amide
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 4167.58
Aliphatic_Index 58.10811
Aromaticity 0.13514
Average_Rotatable_Bonds 3.70270
Charge_at_pH_7 0.08838
Isoelectric_Point 7.53416
Number_of_Hydrogen_Bond_Acceptors 61
Number_of_Hydrogen_Bond_Donors 65
Topological_Polar_Surface_Area 1812.00000
X_logP_energy -21.33606
Interaction Information
Affinity KD=25 nM
Affinity_Assay radioligand binding assay
PDB_ID None
Type Agonist
Structure
Reference Information
Document_Type Research Articles
Title Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase.
Release_Year 1994
PMID None
DOI 10.1016/0169-6009(93)00650-R