1mm9
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(New page: 200px<br /><applet load="1mm9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mm9, resolution 1.66Å" /> '''Streptavidin Mutant ...)
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Revision as of 19:24, 20 November 2007
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Streptavidin Mutant with Insertion of Fibronectin Hexapeptide, including RGD
Overview
The RGD (arginine-glycine-aspartic acid) sequence is found in several, important extracellular matrix proteins and serves as an adhesion ligand, for members of the integrin family of cell-surface receptors. This, sequence and flanking residues from fibronectin or osteopontin have been, engineered into an accessible surface loop of streptavidin to create two, new streptavidin variants (FN-SA or OPN-SA, respectively) that bind cells, through the alpha(v)beta(3) and/or alpha(5)beta(1) integrin receptors., Their crystal structures confirm the design and construction of the, mutants and provide evidence about the conformational dynamics of the RGD, loops. The loops in the isomorphous crystal structures are involved in, crystal-packing interactions and this stabilizes their structures. Even, so, the loop in OPN-SA is slightly disordered and two of the residues are, not seen in difference electron-density maps. Comparison with other, experimentally determined structures of RGD loops in cell-adhesion, molecules shows that these loops occupy a large subset of conformational, space. This is consistent with the view that RGD loops, at least those, involved in cell adhesion, sample a number of structures dynamically, a, few of which display high affinity for appropriate receptors.
About this Structure
1MM9 is a Single protein structure of sequence from Streptomyces avidinii with MRD as ligand. Full crystallographic information is available from OCA.
Reference
Structural characterization and comparison of RGD cell-adhesion recognition sites engineered into streptavidin., Le Trong I, McDevitt TC, Nelson KE, Stayton PS, Stenkamp RE, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):828-34. Epub 2003, Apr 25. PMID:12777798
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