Primary Information | |
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BoMiProt ID | Bomi3197 |
Protein Name | Pancreatic trypsin inhibitor |
Organism | Bos taurus |
Uniprot ID | P00974 |
Milk Fraction | Whey |
Aminoacid Length | 100 |
Molecular Weight | 10903 |
FASTA Sequence | Download |
Protein Existence Status | Reveiwed:Experimental evidence at protein level |
Secondary Information | |
Protein Function | Bovine basic pancreatic trypsin inhibitor (BPTI), and trypsin-kallikrein inhibitor, is one of the most extensively studied globular proteins. BPTI has a relatively broad specificity, inhibiting trypsin- as well as chymotrypsin- and elastase-like serine (pro)enzymes endowed with very different primary specificity. |
Biochemical Properties | Monomeric BPTI shows a very compact pear-shaped structure. The reactive site bond in BPTI is that between Lys15(P1) and Ala16(P1’) at the narrow end of the molecule. The relatively small hydrophobic core of BPTI consists of the side chains of the following residues:Phe4, Cys5-Cys55, Phe22, Tyr23, Cys30-Cys51, Phe33,Tyr35, and Phe45. Decameric BPTI resembles a compact globular particle where ten BPTI subunits are organized in the uncommon 52 point group symmetry (i.e., orthogonal 5-fold and 2-fold axes). Interestingly, the reactive sites of BPTI subunits are facing the central pore of the decamer. |
PTMs | Disulfide bond formation |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
Predicted Disorder Regions | 1-9,27-28,96-100 |
DisProt Annotation | Disorder content 25% Term molten globule, Fragment 14 - 38 Term protein binding, Fragment 14 - 38 Term molecular function inhibitor activity,Fragment 14 - 38 |
TM Helix Prediction | No TM helices |
Significance of PTMs | Disulfide bonds link half-cystine residues 5 and 55, 14 and 38, and 30 and 51. |
PDB ID | 1AAL, 1B0C, 1BHC, 1BPI, 1BPT, 1BRB, 1BTH, 1BTI, 1BZ5, 1BZX, 1CBW, 1CO7, 1D0D, 1EAW, 1EJM, 1F5R, 1F7Z, 1FAK, 1FAN, 1FY8, 1G6X, 1JV8, 1JV9, 1K09, 1K6U, 1LD5, 1LD6, 1MTN, 1NAG, 1OA5, 1OA6, 1P2I, 1P2J, 1P2K, 1P2M, 1P2N, 1P2O, 1P2Q, 1PIT, 1QLQ, 1T7C, 1T8L, 1T8M, 1T8N, 1T8O, 1TPA, 1UUA, 1UUB, 1YKT, 1YLC, 1YLD, 2FI3, 2FI4, 2FI5, 2FTL, 2FTM, 2HEX, 2IJO, 2KAI, 2PTC, 2R9P, 2RA3, 2TGP, 2TPI, 2ZJX, 2ZVX, 3BTD,3BTE, 3BTF, 3BTG, 3BTH, 3BTK, 3BTM,3BTQ, 3BTT, 3BTW, 3FP6, 3FP7, 3FP8, 3GYM, 3LDI, 3LDJ, 3LDM, |
Bibliography | 1.Ascenzi P, Bocedi A, Bolognesi M, Spallarossa A, Coletta M, De Cristofaro R, Menegatti E. The bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor): a milestone protein. Curr Protein Pept Sci. 2003 Jun;4(3):231-51. doi: 10.2174/1389203033487180. PMID: 12769721. 2.Anderer FA, Hörnle S. The disulfide linkages in kallikrein inactivator of bovine lung. J Biol Chem. 1966 Apr 10;241(7):1568-72. PMID: 5296424. |