BOVINE ALPHA-CHYMOTRYPSIN:BPTI CRYSTALLIZATIONBOVINE ALPHA-CHYMOTRYPSIN:BPTI CRYSTALLIZATION

Structural highlights

1mtn is a 8 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CTRA_BOVIN

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of bovine alpha-chymotrypsin (alpha-CHT) in complex with the bovine basic pancreatic trypsin inhibitor (BPTI) has been solved and refined at 2.8 A resolution (R-factor = 0.18). The proteinase:inhibitor complex forms a compact dimer (two alpha-CHT and two BPTI molecules), which may be stabilized by surface-bound sulphate ions, in the crystalline state. Each BPTI molecule, at opposite ends, is contacting both proteinase molecules in the dimer, through the reactive site loop and through residues next to the inhibitor's C-terminal region. Specific recognition between alpha-CHT and BPTI occurs at the (re)active site interface according to structural rules inferred from the analysis of homologous serine proteinase:inhibitor complexes. Lys15, the P1 residue of BPTI, however, does not occupy the alpha-CHT S1 specificity pocket, being hydrogen bonded to backbone atoms of the enzyme surface residues Gly216 and Ser217.

Crystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites.,Capasso C, Rizzi M, Menegatti E, Ascenzi P, Bolognesi M J Mol Recognit. 1997 Jan-Feb;10(1):26-35. PMID:9179777[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Capasso C, Rizzi M, Menegatti E, Ascenzi P, Bolognesi M. Crystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites. J Mol Recognit. 1997 Jan-Feb;10(1):26-35. PMID:9179777 doi:<26::AID-JMR351>3.0.CO;2-N 10.1002/(SICI)1099-1352(199701/02)10:1<26::AID-JMR351>3.0.CO;2-N

1mtn, resolution 2.80Å

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