 |
PDBsum entry 1mct
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Hydrolase/hydrolase inhibitor
|
PDB id
|
|
|
|
1mct
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Refined 1.6 a resolution crystal structure of the complex formed between porcine beta-Trypsin and mcti-A, A trypsin inhibitor of the squash family. Detailed comparison with bovine beta-Trypsin and its complex.
|
|
|
Authors
|
|
Q.Huang,
S.Liu,
Y.Tang.
|
|
|
Ref.
|
|
J Mol Biol, 1993,
229,
1022-1036.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The crystal structure of the complex formed by porcine beta-trypsin with the
MCTI-A inhibitor (Momordica charantia, Linn. Cucurbitaceae) has been determined
at 1.6 A resolution using the molecular replacement method. The sequence of
MCTI-A was determined by recognizing the electron density, and shows that MCTI-A
is a member of the squash family of trypsin inhibitors. We report the first
high-resolution structure of porcine beta-trypsin. Detailed comparisons have
been made on the overall structure, solvent structure and active-site geometries
between this complex and bovine beta-trypsin and its complexes. On the basis of
our results, we discuss the interaction patterns between inhibitor and trypsin.
Unlike other complex structures formed by bovine trypsin with inhibitors, no
out-of-plane distortion around the inhibitor's scissible peptide was observed.
The role of the trypsin catalytic triad is also discussed on the basis of this
structure.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Amino acid sequencing of a trypsin inhibitor by refined 1.6 a X-Ray crystal structure of its complex with porcine beta-Trypsin.
|
|
|
Authors
|
|
Q.Huang,
S.Liu,
Y.Tang,
F.Zeng,
R.Qian.
|
|
|
Ref.
|
|
FEBS Lett, 1992,
297,
143-146.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
