Binding structural biology

Curry, S., Mandelkow, H., Brick, P. and Franks, N. (1998) Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nature Structural Biology 5, 827-835. 

Gelb, M.H., Cho, W. and Wilton, D.C. (1999) Interfacial binding of secreted phospholipase A2 more than electrostatics and a major role for tryptophan. Current Opinion in Structural Biology 9, 428-432. 

Insect OBPs are secretory proteins whose only posttranslational modification is the formation of three disulfide bridges [39,45] from six cysteine residues. That six cysteine residues are well conserved in OBPs from species of the same order is a hallmark of these proteins. The disulfide links of OBPs in a few species have been determined by analytical methods, first in the OBPs from B. mori [45,46]. As part of our attempt to get better insight into the structural biology of pheromone-binding proteins, we have determined the disulfide linkages... 

Qiu, C., Sawada, K., Zhang, X. and Cheng, X. (2002) The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds. Nature Structural Biology, 9, 217-224. 

Kozbial, P.Z. and Mushegian, A.R. (2005) Natural history of S-adenosyhnethionine-binding proteins. BMC Structural Biology, 5, 19. 

Also related to Src kinase structural biology have been studies on two SFKs, namely Lck and Fyn. Importantly, the X-ray structure of Lck kinase was the first SFK determined [64] as complexes with AMP-PNP, staurosporine and PP2. Furthermore, a Fyn kinase-staurosporine complex has been recently described [65]. Extrapolating from the above Src kinase inhibitor crystal structures with respect to the hydrophobic specificity pocket and the active conformation of the protein to bind ATP-competitive inhibitors of varying templates and functional group elaboration, a working hypothesis of known Src kinase inhibitors (vide infra) can be suggested (Fig. 4). 

DeLano, W. L. (2002). Unraveling hot spots in binding interfaces progress and challenges. Current Opinions in Structural Biology 12, 14—20. 

As a result, 10 additional compounds were added to obtain the final training set constituted by a total of 24 structures. Biological data associated with these compounds, expressed as Kit ranged between 0.21 nM, found for compound 5, and 2396 nM, found for compound 7 (Table 12.1). We assumed that all these compounds were acting through the same mechanism of action at the same binding site. 

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