1F2S

CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPSIN AND MCTI-A, A TRYPSIN INHIBITOR OF SQUASH FAMILY AT 1.8 A RESOLUTION

Replaces:  1MCU

Summary for 1F2S

• Entry DOI: 10.2210/pdb1f2s/pdb
• Related: 1MCT
• Descriptor: TRYPSIN, TRYPSIN INHIBITOR A, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: proteinase-inhibitor complex, trypsin, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Bos taurus (cattle); More
• Cellular location: Secreted, extracellular space: P00760; Secreted: P10295
• Total number of polymer chains: 2
• Total formula weight: 26616.32

Authors

Zhu, Y.,Huang, Q.,Qian, M.,Jia, Y.,Tang, Y. (deposition date: 2000-05-29, release date: 2000-06-05, Last modification date: 2024-10-16)

Primary citation

Zhu, Y.,Huang, Q.,Qian, M.,Jia, Y.,Tang, Y.
Crystal structure of the complex formed between bovine beta-trypsin and MCTI-A, a trypsin inhibitor of squash family, at 1.8-A resolution.
J.Protein Chem., 18:505-509, 1999

PubMed Abstract: The stoichiometric complex formed between bovine beta-trypsin and Momordica charantia, Linn. Cucurbitaceae trypsin inhibitor A (MCTI-A) was crystallized and its X-ray crystal structure was refined to a final R value of 0.179 using data of 7.0- to 1.8-A resolution. Combination with results on the complex of MCTI-A with porcine trypsin gives the sequence of MCTI-A definitely, of which 13 residues are conserved compared with other squash family trypsin inhibitors. Its spatial structure and the conformation of its primary binding segment from Cys3I (P3) to Glu7I (P3'), which contains a reactive scissile bond Arg5I C-Ile6I N, were found to be very similar to the other squash family proteinase inhibitors.

PubMed: 10524768
DOI: 10.1023/A:1020690931043

Experimental method

X-RAY DIFFRACTION (1.79 Å)