1mm9 | pdb_00001mm9

Streptavidin Mutant with Insertion of Fibronectin Hexapeptide, including RGD

spinqualitylabelsall models 1mm9, resolution 1.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1mm9 is a 1 chain structure with sequence from As 4.1583. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MRD Related: 1swe, 1mk5, 1mep Gene: core streptavidin (AS 4.1583) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Avidin 3D structures

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