Chymotrypsin Inhibitor

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Function

Chymotrypsin Inhibitors (CI) are serine proteinase inhibitors of chymotrypsin. They are classified by numbers: CI-1[1], CI-2[2], CI-3[3]. Subtilisin-chymotrypsin inhibitor inhibits both subtilisin and chymotrypsin.

Structural highlights

CI inhibition is achieved by the insertion of a loop into the serine protease active site. [4]

3D Structures of Chymotrypsin inhibitor

Chymotrypsin inhibitor 3D structures


Chymotrypsin Inhibitor 2 (cyan) complex with subtilisin (magenta), PEG, citrate, Ca+2 (green) and Na+ (purple) ions (PDB entry 1to1)

Drag the structure with the mouse to rotate

References

  1. Huang K, Strynadka NC, Bernard VD, Peanasky RJ, James MN. The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure. 1994 Jul 15;2(7):679-89. PMID:7922044
  2. McPhalen CA, James MN. Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds. Biochemistry. 1987 Jan 13;26(1):261-9. PMID:3828302
  3. Ravichandran S, Sen U, Chakrabarti C, Dattagupta JK. Cryocrystallography of a Kunitz-type serine protease inhibitor: the 90 K structure of winged bean chymotrypsin inhibitor (WCI) at 2.13 A resolution. Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1814-21. PMID:10531477
  4. Radisky ES, Kwan G, Karen Lu CJ, Koshland DE Jr. Binding, proteolytic, and crystallographic analyses of mutations at the protease-inhibitor interface of the subtilisin BPN'/chymotrypsin inhibitor 2 complex. Biochemistry. 2004 Nov 2;43(43):13648-56. PMID:15504027 doi:http://dx.doi.org/10.1021/bi048797k

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