Globular head

Figure S.21 The hemaggiutinin moiecuie is formed from three subunits. Each of these subunits Is anchored In the membrane of the influenza vims. The globular heads contain the receptor sites that bind to sialic acid residues on the surface of eukaryotic cells. A major part of the subunit interface is formed by the three long intertwining helices, one from each subunit. (Adapted from I. Wilson et al.. Nature 289 366-373, 1981.)...

Figure 5.23 The globular head of the hemagglutinin subunit Is a distorted jelly roll stmcture (a). P strand 1 contains a long Insertion, and P strand 8 contains a bulge in the corresponding position. Each of these two strands is therefore subdivided Into shorter P strands. The loop region between P strands 3 and 4 contains a short a helix, which forms one side of the receptor binding site (yellow circle). A schematic diagram (b) Illustrates the organization of the p strands into a jelly roll motif.

Figure 14.14 Sci ematic diagram of the myosin molecule, comprising two heavy chains (green) that form a coiled-coil tail with two globular heads and four light chains (gray) of two slightly differing sizes, each one bound to each heavy-chain globular head.

Even though dynein, kinesin, and myosin serve similar ATPase-dependent chemomechanical functions and have structural similarities, they do not appear to be related to each other in molecular terms. Their similarity lies in the overall shape of the molecule, which is composed of a pair of globular heads that bind microtubules and a fan-shaped tail piece (not present in myosin) that is suspected to carry the attachment site for membranous vesicles and other cytoplasmic components transported by MT. The cytoplasmic and axonemal dyneins are similar in structure (Hirokawa et al., 1989 Holzbaur and Vallee, 1994). Current studies on mutant phenotypes are likely to lead to a better understanding of the cellular roles of molecular motor proteins and their mechanisms of action (Endow and Titus, 1992). 

Joseph K, Ghebrehiwet B. Peerschke El. Reid KB. Kaplan AP Identification of the zinc-dependent endothelial cell binding protein for high molecular weight kininogen and factor Xll identity with the receptor that binds to the globular heads of Clq (gClq-R). Proc Natl Acad Sci USA 1996 93 8552-8557. 

The T4 short tail fiber triple /l-helix is connected to a more globular head domain via residues 333-341, which form a very short a-helical triple coiled-coil. Residues 342-396, together with the C-terminal /1-strand composed of amino acids 518-527 (the collar ), are the only part of the structure in which the monomer has a recognizable fold. It may therefore be the first part of the protein to fold, followed by a zipping-up of the N-terminal domain and the top domain. The small, globular, domain contains six /1-strands and one a-helix and has some structural homology to gpl 1, also of bacteriophage T4. Three of the /1-strands and the a-helix formed by residues... 

The condensin complex has been identified in the same scaffold fraction (Maeshima and Laemmli, 2003) and shown to be essential for the mitotic chromosome condensation (Hirano et al, 1997). The frog condensin complex exhibits ATP-dependent DNA-supercoiling activity (Kimura and Hirano, 1997). It consists of a heterodimer of SMC and a trimer of non-SMC proteins (Hirano et al, 1997). The SMC complex has a globular head domain and a coiled-coil tail region (Anderson et al., 2002 Melby et al, 1998 Yoshimura et al., 2002). In vertebrates, two types of condensin complex, condensin I and condensin II, exist they are composed of the same SMC subunits but with different non-SMC subunits (Ono et al, 2003). 

It is a large protein that consists of six polypeptide chains, two identical heavy chains (each 220 kDa) and two pairs of light chains (each -20 kDa). The two heavy chains form a long coiled unit known as the tail, which associates laterally with other myosin molecules to form the thick filament. At one end of the chain are the two globular heads which form the crossbridges. Each head has two domains, one on either side. 

Myosin is quantitatively the most important protein in the myofibrils, representing 65% of the total. It is shaped like a golf club (bottom right). The molecule is a hexamer consisting of two identical heavy chains (2 X 223 kDa) and four light chains (each about 20 kDa). Each of the two heavy chains has a globular head at its amino end, which extends into a tail about 150 nm long in which the two chains are intertwined to form a superhelix. The small subunits are attached in the head area. Myosin is present as a bundle of several hundred stacked molecules in the form of a thick myosin filament. The head portion of the molecule acts as an ATPase, the activity of which is modulated by the small subunits. 

Comparison of all known sequences of approximately 390 residues of the neuraminidase globular head [24], indicates that only 54 (excluding 16 conserved cysteine residues) are invariant (Figure 5a). Apart from 21 residues involved... 

Additional information <1-3, 5, 6, 8, 10, 11> (<1> gel electrophoresis in various buffers gives different molecular weights [3] <1-3, 8> skeletal muscle enzyme structure overall asymmetric shape, globular head and tail region... 

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