Dynamic Hinge Regions co-localize with Biological Important Residues of 25 Proteins

  Abstract

We have investigated different global motions in the computed dynamic fluctuations exhibited by twenty five proteins with a coarse-grained Gaussian network model. Meanwhile, we compare the residues in structural stable hinge regions with biological critical residues including active sites and inhibitor binding sites which were mentioned in the literature. After randomly choosing 25 proteins from the Brookhaven Protein Databank (PDB), we found biological catalytic residues and inhibitor binding residues highly colocalized in the dynamic hinge region of proteins.


Click on Image to view Slide Presentation

Paper (.doc)

Fig2-fluctuation profiles (.pdf)


Supplement 1
(.doc)


Supplement 2
(.doc)

Table 1. Description of 24 test proteins (.doc)

Table 2 (.xls)

Color-coded ribbon diagrams for test proteins (.doc)

 

 

University of Pittsburgh ---------- School of Medicine
3064 Biomedical Science Tower  3501 Fifth Ave., Pittsburgh, PA 15213.     Phone : (412) 648-3333,  Fax: (412) 648-3163

Tel : (412) 648-6671,  Fax: (412) 648-6676