 |
PDBsum entry 1vfl
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Structural basis of compound recognition by adenosine deaminase.
|
|
|
Authors
|
|
T.Kinoshita,
I.Nakanishi,
T.Terasaka,
M.Kuno,
N.Seki,
M.Warizaya,
H.Matsumura,
T.Inoue,
K.Takano,
H.Adachi,
Y.Mori,
T.Fujii.
|
|
|
Ref.
|
|
Biochemistry, 2005,
44,
10562-10569.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Structural snapshots corresponding to various states enable elucidation of the
molecular recognition mechanism of enzymes. Adenosine deaminase has two distinct
conformations, an open form and a closed form, although it has so far been
unclear what factors influence adaptation of the alternative conformations.
Herein, we have determined the first nonligated structure as an initial state,
which was the open form, and have thereby rationally deduced the molecular
recognition mechanism. Inspection of the active site in the nonligated and
ligated states indicated that occupancy at one of the water-binding positions in
the nonligated state was highly significant in determining alternate
conformations. When this position is empty, subsequent movement of Phe65 toward
the space induces the closed form. On the other hand, while occupied, the
overall conformation remains in the open form. This structural understanding
should greatly assist structure-oriented drug design and enable control of the
enzymatic activity.
|
|
|
|
|
|
|
