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Fig. 6.18 The 3SDH protein: 3D representation ( top ) with ligand binding residues marked in yel-
low and the complexation interface marked in magenta . Ligands are given in red . Local
Δ H
profile maxima are marked in yellow . All colors correspond to the bottom graph, which shows the
actual
Δ H pro fi le for 3SDH
a ligand), it becomes difficult to distinguish one distortion from the other. Thus,
accurate prediction of ligand binding and protein complexation sites depends on
measuring the relative significance of each factor.
For the sample protein designated 1G8M (transferase, hydrolase - crystal structure
of avian atic, a bifunctional transformylase and cyclohydrolase enzyme in purine bio-
synthesis - EC 2.1.2.3, EC 3.5.4.10) (Greasley et al. 2001 ) the “fuzzy oil drop” model was
able to correctly identify the complexation site (by locating residues which represent
local maxima of the
Δ H profile). However, this protein is also capable of binding a
ligand (speci fi cally, C 10 H 14 N 5 O 8 P - Guanosine-5¢-monophosphate). Identifying this
ligand's binding pocket would likely prove difficult as the deformation triggered by
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