 |
PDBsum entry 2iln
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Hydrolase/hydrolase inhibitor
|
PDB id
|
|
|
|
2iln
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Hydrolase/hydrolase inhibitor
|
|
|
Title:
|
|
Crystal structure of the bowman-birk inhibitor from snail medic seeds in complex with bovine trypsin
|
|
Structure:
|
|
Cationic trypsin. Chain: a, b. Synonym: trypsinogen, beta-trypsin. Bowman-birk type proteinase inhibitor. Chain: i. Synonym: msti
|
|
Source:
|
|
Bos taurus. Cattle. Organism_taxid: 9913. Tissue: pancreas. Medicago scutellata. Organism_taxid: 36901. Tissue: seed
|
|
Resolution:
|
|
|
2.00Å
|
R-factor:
|
0.235
|
R-free:
|
0.287
|
|
|
Authors:
|
|
S.Capaldi,M.Perduca,B.Faggion,M.E.Carrizo,A.Tava,L.Ragona,H.L.Monaco
|
|
Key ref:
|
|
S.Capaldi
et al.
(2007).
Crystal structure of the anticarcinogenic Bowman-Birk inhibitor from snail medic (Medicago scutellata) seeds complexed with bovine trypsin.
J Struct Biol,
158,
71-79.
PubMed id:
|
|
|
Date:
|
|
|
03-Oct-06
|
Release date:
|
10-Apr-07
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
Chains A, B:
E.C.3.4.21.4
- trypsin.
|
|
|
|
|
|
|
Reaction:
|
|
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
J Struct Biol
158:71-79
(2007)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Crystal structure of the anticarcinogenic Bowman-Birk inhibitor from snail medic (Medicago scutellata) seeds complexed with bovine trypsin.
|
|
S.Capaldi,
M.Perduca,
B.Faggion,
M.E.Carrizo,
A.Tava,
L.Ragona,
H.L.Monaco.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
The structure of the ternary complex of the anticarcinogenic Bowman-Birk
protease inhibitor purified from snail medic (Medicago scutellata) seeds (MSTI)
and two molecules of bovine trypsin has been solved by X-ray diffraction
analysis of single crystals to a resolution of 2.0 A. This is the highest
resolution model of a ternary complex of this type currently available. The two
binding loops of the MSTI differ in only one amino acid and have in both cases
an arginine in position P1. The distances between the residues of the inhibitor
at the binding interface and the trypsin side chains that recognize them are
almost identical in the two sites. When compared to the NMR model of the
uncomplexed MSTI, the inhibitor in the functional assembly with trypsin shows
the largest differences in the two P2' residues. Compared with the similar
ternary complex of the soybean trypsin inhibitor, this model shows very small
differences in the polypeptide chain of the trypsin binding sites and its
largest difference in the area between Asp 26 and His 32 of the MSTI which in
the soybean inhibitor has an extra Leu inserted in position 29.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
C.Cogliati,
S.Tomaselli,
M.Assfalg,
M.Pedò,
P.Ferranti,
L.Zetta,
H.Molinari,
and
L.Ragona
(2009).
Disulfide bridge regulates ligand-binding site selectivity in liver bile acid-binding proteins.
|
| |
FEBS J,
276,
6011-6023.
|
|
|
|
|
|
|
R.Bao,
C.Z.Zhou,
C.Jiang,
S.X.Lin,
C.W.Chi,
and
Y.Chen
(2009).
The ternary structure of the double-headed arrowhead protease inhibitor API-A complexed with two trypsins reveals a novel reactive site conformation.
|
| |
J Biol Chem,
284,
26676-26684.
|
|
|
|
|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
|
|
|
Links
