1TAB

STRUCTURE OF THE TRYPSIN-BINDING DOMAIN OF BOWMAN-BIRK TYPE PROTEASE INHIBITOR AND ITS INTERACTION WITH TRYPSIN

Summary for 1TAB

• Entry DOI: 10.2210/pdb1tab/pdb
• Descriptor: TRYPSIN, BOWMAN-BIRK TYPE PROTEINASE INHIBITOR (3 entities in total)
• Functional Keywords: serine proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Bos taurus (cow)
• Cellular location: Secreted, extracellular space: P00760
• Total number of polymer chains: 2
• Total formula weight: 32466.41

Authors

Tsunogae, Y.,Tanaka, I.,Yamane, T.,Kikkawa, J.-I.,Ashida, T.,Ishikawa, C.,Watanabe, K.,Nakamura, S.,Takahashi, K. (deposition date: 1990-10-15, release date: 1992-01-15, Last modification date: 2024-06-05)

Primary citation

Tsunogae, Y.,Tanaka, I.,Yamane, T.,Kikkawa, J.,Ashida, T.,Ishikawa, C.,Watanabe, K.,Nakamura, S.,Takahashi, K.
Structure of the trypsin-binding domain of Bowman-Birk type protease inhibitor and its interaction with trypsin.
J.Biochem.(Tokyo), 100:1637-1646, 1986

PubMed Abstract: The crystal structure of the complex formed by bovine trypsin and Bowman-Birk type protease inhibitor AB-I extracted from azuki beans (Vigna angularis) 'Takara' has been analyzed. The structure was solved by the application of the phase combination of single isomorphous phases and trypsin model phases, followed by phase improvement using the iterative Fourier technique. From the resulting electron density map, a three-dimensional atomic model of the trypsin binding domain of AB-I has been built. The peptide chain at the trypsin reactive site turns back sharply at Pro29 and forms a 9-residue ring (Cys24-Cys32). The 'front side' of this ring, consisting of the reactive site (Cys24-Met28), interacts with trypsin in a similar manner to other families of inhibitors and forms a stable complex, which seems to be maintained by the interactions with the 'back side' of this ring (Pro29-Cys34). The similar spatial arrangements of the 'back side' of this inhibitor and the 'secondary contact region' of the other inhibitors with respect to the reactive site suggest an important common role of these regions in exhibiting inhibitory activity.

PubMed: 3032921

Experimental method

X-RAY DIFFRACTION (2.3 Å)