Fibronectin type III domain

Figure 13.19 Ribbon diagram of the stmcture of the extracellular domain of the human growth hormone. The hormone-binding region is formed by loops (yellow) at the hinge region between two fibronectin type III domains. (Adapted from J. Wells et al., Annu. Rev.

Figure 15.24 Ribbon diagram (a) and topology diagram (b) of the fibronectin type III domain, which is composed of a three-stranded and a four-stranded p sheet packed together as a compressed barrel.

From Guss and Freeman.116 (B) Ribbon drawing of immunoglobulin fold. This is a common structure in domains of the immunoglobulins and in many other extracellular proteins. Two layers of antiparallel (3 sheet are stacked face to face to form a flattened barrel. One disulfide bridge is always present and is represented as a thick rod. From J. Richardson.117 (C) Five tandem fibronectin type III domains. 

Q Fibronectin type III domain (motif I) Q MLCK region [] Immunoglobulin domain (motif II) Q Interdomain... 

Leahy, D. J., Hendrickson, W. A., Aukhil, L, and Erickson, H. P. (1992). Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the seleno-methionyl protein. Science 258, 987-991. 

IL-IOR is a single-chain receptor. IL-IOR belongs to the class II cytokine receptor family that also includes the IFN receptors (IFNy and IFNap receptors). The extracellular region consists of two homologous fibronectin type III domains that are without the WSXWS motif characteristic of class I cytokine receptors. It is expressed on B cells, thymocytes, and other cellular lines such as mast cells and macrophages. Human IL-IOR mRNA is restricted mostly to hematopoietic cells and cell lines. ... 

Lipovsek, D., Lippow, S. M., Hackel, B. J., Gregson, M. W., Cheng, P., Kapila, A. and Wittrup, K D. (2007) Evolution of an interloop disulfide bond in high-affinity antibody mimics based on fibronectin type III domain and selected by yeast surface display molecular convergence with single-domain camelid and shark antibodies. J Mol Biol 368, 1024-1041... 

Fig. 17. The structure of the neuroglian and fasciclin II and III proteins, as deduced from their DNA sequences. Each possesses several immunoglobulin domains, a protein structure found in a variety of cell adhesion and immunoglobulin molecules in vertebrates. The neuroglian and fasciclin II proteins also possess a number of fibronectin type III domains. All three proteins exist in a transmembrane form with a cytoplasmic domain, while fasciclin II also appears to exist in a phosphotidylinositol-linked form (reproduced, with permission, from the Annual Review of Cell Biology, Vol. 7, 1991 by Annual Reviews Inc.).

Fig. 2. The interaction between ligands (cytokines) and receptors of the IL-6 family is schematically shown. Only cytokine domains and fibronectin type III domains are shown. References Taga and Kishimoto (1992) Stahl and Yancopoulos (1993).

Figure 9.53. Stereo views of a fibronectin type III domain of tenascin with aromatics (black), other hydrophobics (gray), neutrals (light gray), and charged residues (white). (A) Ribbon representation showing seven P-strands and the turn containing the GRGDSP cell attachment site that in our designed...

Eight p-chains are known, and they display 37-55 % sequence homology. More than W % of the p-chain is extracellular, and it displays a highly conserved pattern of Cys residues and four repeals of a Cys-tich domain. Its cytoplasmic domain (40-50 residues) often carries a phosphorylatable Tyr residue. p4 has an exceptionally Icmg cytoplasmic t of about 1000 amino acids, containing 4 fibronectin type III domains. 

Human GM-CSF receptor is composed of at least 2 subunits the 3-subunit is identical with a subunit of the receptors for interleukin-3 and interleukin-5. Both subunits have domains that are structurally related to a fibronectin type III domain, a structure that is conserved in all members of the cytokine receptor superfamily. Genomic DNA clones containing the entire coding sequence of the a-subunit have been isolated and characterized [Y.Nakagawa etal. J. Biol. Chem. 269 (1994) 10905-10912). 

Self-consistent Determination of the Transition State for Protein Folding Application to a Fibronectin Type III Domain. 

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