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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In particular, a conserved hydrophobic residue protrudes from the ECH in one protomer and snugly fits into a hydrophobic pocket formed by conserved residues in TM3 and ECS2 of 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.
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 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.
The replaced amino acids were located in a refined 3-dimensional computer model of the HAV protomer (11), and their relative distances to residues 1102, 1171 and 1176, constituents of the immunodominant site (12), and to residue 1221, constituent of the glycophorin A binding site epitope (13), were used as markers of the potential antibody-escaping phenotype.
GltPh is a trimer in which each protomer functions independently of the others.
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.
The secreted mature toxin, or protomer, is a hydrophilic molecule that lacks cysteine residues and has a molecular mass of approximately 33 kDa (6-8).
The functional CRP protomer is composed of two molecules of CRP, each being associated with cAMP.
The structure of CRP contains a crystal contact where the calcium-binding loop from one protomer coordinates into the calcium site of a second protomer to form the pentameric structure (Fig.
They are amongst the largest ion channels, comprised of the four identical ~565 kDa channel-forming protomers.
On the other face of CRP (the A face), the 5 protomers cooperatively form a single larger binding site that can accommodate both complement protein C1q (1, 11) and various Fc receptors (1, 12).