protomer


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protomer

[′prōd·ə·mər]
(biochemistry)
One of the polypeptide chains composing an oligomeric protein. Also known as subunit.
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References in periodicals archive ?
Bond, "Multimeric structure of the secreted meprin a metalloproteinase and characterization of the functional protomer," The Journal of Biological Chemistry, vol.
PTX3 is composed of eight identical protomer subunits by disulfide bonds and is a member of the highly conserved pentraxin superfamily.
The union takes place in each of the "binding sites" located in the protomer units that the oligomer possesses.
12F, a tight junction strand formed by the conserved hydrophobic residue that protrudes from the ECH in one protomer fits snugly into the hydrophobic pocket formed by TM3 and ECS2 in the adjacent protomer (Fig.
The prototypical protomer is thought to have evolved from an internal duplication and inversion of a trihelical-transmembrane segment causing the mature peptide to retain intracellular N- and C-termini of variable length and conformation (Pao et al., 1991).
Structurally, FHIT forms a dimer in solution (PDB code: l FIT) and general structure of its protomer can be described as a common [alpha]+[beta] type (15).
The 3D structure uncovered by Korennykh and his team consists of two nearly identical subunits called protomers. The initial protomer latches onto one of the four "letters" that make up the RNA code, in particular, the "U," which stands for a component of RNA called uridine.
In this state, the protomer configuration resembles that of the soluble monomer, and the whole oligomer still stands prone to the membrane with an intact lipid bilayer beneath the assembled ring.
This hypothesis is substantiated by the fact that when the 100,000[g.sub.av] x 90 min fraction is prepared from mammary gland homogenized in the presence of avidin (protomer not activated by citrate during assay), the activities of acetyl-CoA carboxylase were very low (Table 4).
(6) A tropomyosin molecule is thought to be a canonical coiled-coil protein, about 40 nm in length, which binds to actin filament covering seven contiguous actin protomers (monomers), (7) with the length of an actin protomer being about 5.5 nm.