 |
PDBsum entry 2ci2
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Proteinase inhibitor (chymotrypsin)
|
PDB id
|
|
|
|
2ci2
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal and molecular structure of the serine proteinase inhibitor ci-2 from barley seeds.
|
|
|
Authors
|
|
C.A.Mcphalen,
M.N.James.
|
|
|
Ref.
|
|
Biochemistry, 1987,
26,
261-269.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Chymotrypsin inhibitor 2 (CI-2), a serine proteinase inhibitor from barley
seeds, has been crystallized and its three-dimensional structure determined at
2.0-A resolution by the molecular replacement method. The structure has been
refined by restrained-parameter least-squares methods to a crystallographic R
factor (= sigma parallel Fo magnitude of-Fo parallel/sigma magnitude of Fo) o of
0.198. CI-2 is a member of the potato inhibitor 1 family. It lacks the
characteristic stabilizing disulfide bonds of most other members of serine
proteinase inhibitor families. The body of CI-2 shows few conformational changes
between the free inhibitor and the previously reported structure of CI-2 in
complex with subtilisin Novo [McPhalen, C.A., Svendsen, I., Jonassen, I., &
James, M.N.G. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 7242-7246]. However, the
reactive site loop has some significant conformational differences between the
free inhibitor and its complexed form. The residues in this segment of
polypeptide exhibit relatively large thermal motion parameters and some disorder
in the uncomplexed form of the inhibitor. The reactive site bond is between
Met-59I and Glu-60I in the consecutive sequential numbering of CI-2
(Met-60-Glu-61 according to the alignment of Svendsen et al. [Svendsen, I.,
Hejgaard, J., & Chavan, J.K. (1984) Carlsberg Res. Commun. 49, 493-502]).
The network of hydrogen bonds and electrostatic interactions stabilizing the
conformation of the reactive site loop is much less extensive in the free than
in the complexed inhibitor.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Comparison of the solution and X-Ray structures of barley serine proteinase inhibitor 2.
|
|
|
Authors
|
|
G.M.Clore,
A.M.Gronenborn,
M.N.James,
M.Kjaer,
C.A.Mcphalen,
F.M.Poulsen.
|
|
|
Ref.
|
|
Protein Eng, 1987,
1,
313-318.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #2
|
|
|
Title
|
|
Crystal and molecular structure of chymotrypsin inhibitor 2 from barley seeds in complex with subtilisin novo.
|
|
|
Authors
|
|
C.A.Mcphalen,
I.Svendsen,
I.Jonassen,
M.N.James.
|
|
|
Ref.
|
|
Proc Natl Acad Sci U S A, 1985,
82,
7242-7246.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #3
|
|
|
Title
|
|
Preliminary crystallographic data for the serine protease inhibitor ci-2 from barley seeds.
|
|
|
Authors
|
|
C.A.Mcphalen,
C.Evans,
K.Hayakawa,
I.Jonassen,
I.Svendsen,
M.N.James.
|
|
|
Ref.
|
|
J Mol Biol, 1983,
168,
445-447.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
