Immunoglobulin binding domain

Ried, M.U., A. Girod, K. Leike, H. Buning, and M. Hallek, Adeno-associated virus capsids displaying immunoglobulin-binding domains permit antibody-mediated vector retargeting to specific cell surface receptors. J Virol, 2002. 76(9) 4559-66. 

Djojonegoro BM, Benedik MJ, Willson RC, Bacteriophage surface display of an immunoglobulin-binding domain of Staphylococcus aureus protein A, BioTechnology, 12 169-172, 1994. 

SpA-derived proteins containing different number and composition of domains have been produced by recombinant methods. The binding properties of intact SpA and some SpA-derived protein fragments to IgG, IgA, IgM, and F(ab )2 have been analyzed. The results suggest that the binding is affected both by the number of immunoglobulin binding domains and by the composition of the domains. 

Ricci S, Medaglini D, Marcotte H, Olsen A, Pozzi G, Bjorck L Immunoglobulin-binding domains of peptostreptococcal protein L enhance vaginal colonization of mice by Streptococcus gordonii. Microb Pathog 2001 30 229-235. 

Beckingham, J. A., Bottomley, S. P., Hinton, R., Sutton, B. J. and Gore, M. G, 1999, Interactions between a single immunoglobulin-binding domain of protein L from Peptostreptococcus magnus and a human k light chain. Biochemical Journal 340, 193-199. 

Franks WT, Zhou DH, Wylie BJ et al (2005) Magic-angle spinning solid-state NMR spectroscopy of the pi immunoglobulin binding domain of protein G (GBl) N and C chemical shift assignments and conformational analysis. J Am Chem Soc 127 12291-12305... 

Figure 9 Thickness of a protein, (a) The structure of the B1 immunoglobulin-binding domain of streptococcal protein G is visualized as a thin tube, (b) View of the same tube inflated to its thickness (i.e., to a radius above which the tube ceases to be smooth, or shows self contact). Note that no free space exists between consecutive turns of the helices. Figure 9a drawn with MOLSCRIPT and 9b with VMD. ...

A. V. Glyakina, N. K. Balabaev, and O. V. Galzitskaya, Biochemistry (Moscow), 74(316) (2009). Comparison of Transition States Obtained Upon Modeling of Unfolding of Immunoglobulin-Binding Domains of Proteins L and G Caused by External Action with Transition States Obtained in the Absence of Force Probed by Experiments. 

The possibility of exploiting enhanced paramagnetic relaxation as an effective source of structural constraints was explored by JarOTiiec and coworkers on microcrystalline samples of a model protein, the B1 immunoglobulin-binding domain of protein G (GBl). Here a solvent-exposed cysteine residue was used to incorporate a thiol-specific paramagnetic nitroxide (TEMPO) or a thiol-specific EDTA-metal reagent bound to Cu and Mn° ions [99-101]. 

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