1FAN

CREVICE-FORMING MUTANTS IN THE RIGID CORE OF BOVINE PANCREATIC TRYPSIN INHIBITOR: CRYSTAL STRUCTURES OF F22A, Y23A, N43G, AND F45A

Summary for 1FAN

• Entry DOI: 10.2210/pdb1fan/pdb
• Descriptor: BOVINE PANCREATIC TRYPSIN INHIBITOR (2 entities in total)
• Functional Keywords: serine protease inhibitor
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 1
• Total formula weight: 6451.47

Authors

Danishefsky, A.T.,Wlodawer, A.,Kim, K.-S.,Tao, F.,Woodward, C. (deposition date: 1992-08-21, release date: 1993-10-31, Last modification date: 2019-08-14)

Primary citation

Danishefsky, A.T.,Housset, D.,Kim, K.S.,Tao, F.,Fuchs, J.,Woodward, C.,Wlodawer, A.
Crevice-forming mutants in the rigid core of bovine pancreatic trypsin inhibitor: crystal structures of F22A, Y23A, N43G, and F45A.
Protein Sci., 2:577-587, 1993

PubMed Abstract: Crystal structures of four mutants of bovine pancreatic trypsin inhibitor (F22A, Y23A, N43G, and F45A), engineered to alter their stability properties, have been determined. The mutated residues, which are highly conserved among Kunitz-type inhibitors, are located in the rigid core of the molecule. Replacement of the partially buried bulky residues of the wild-type protein with smaller residues resulted in crevices open to the exterior of the molecule. The overall three-dimensional structure of these mutants is very similar to that of the wild-type protein and only small rearrangements are observed among the atoms lining the crevices.

PubMed: 8518731

Experimental method

X-RAY DIFFRACTION (2 Å)