The @entity4328 gelation factor shares a putative actin binding site with alpha-actinins and XXXX and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation.

@entity1 @entity1522 @entity2228 @entity35375 @entity4328 @entity1573 @entity4714 @entity1521
The 120-kD gelation factor and @entity35375 are among the most abundant F-actin cross-linking proteins in @entity4328 . Both molecules are homodimers and have extended rod-like configurations that are respectively approximately 35 and 40 nm long. Here we report the complete cDNA sequence of the 120-kD gelation factor which codes for a protein of 857 @entity1522 . Its calculated molecular mass is 92.2 kD which is considerably smaller than suggested by its mobility in SDS-PAGE. Analysis of the sequence shows a region that is highly homologous to @entity4328 @entity35375 , @entity1573 fibroblast @entity35375 , and @entity1 @entity4714 . This conserved domain probably represents an actin binding site that is connected to the rod-forming part of the molecule via a highly charged stretch of @entity1522 . Whereas the sequence of @entity35375 (Noegel, A., W. Witke, and M. Schleicher. 1987. FEBS [Fed. Eur. Biochem. Soc.] Lett. 221:391-396) suggests that the extended rod domain of the molecule is based on four spectrin-like repeats with high alpha-helix potential, the rod domain of the 120-kD gelation factor is constructed from six 100-residue repeats that have a high content of @entity2228 and @entity1521 residues and which, in contrast to @entity35375 , do not appear to have a high alpha-helical content. These repeats show a distinctive pattern of regions that have high beta-sheet potential alternating with short zones rich in residues with a high potential for turns. This observation suggests that each 100-residue motif has a cross-beta conformation with approximately nine sheets arranged perpendicular to the long axis of the molecule. In the high beta-potential zones every second residue is often hydrophobic. In a cross-beta structure, this pattern would result in one side of the domain having a surface rich in hydrophobic side chains which could account for the dimerization of the 120-kD gelation factor subunits.
