calponin

Calponin is mainly made up of α-helices with hydrogen bond turns.

In molecular biology, the calponin family repeat is a 26 amino acid protein domain.

Calponin molecules may exist in equal number as actin, and has been proposed to be a load-bearing protein.

Basaloid or myoepithelial cells: positive with S100 protein, muscle specific actin, calponin and p63.

Calponin is a calcium binding protein.

Calponin is also thought to negatively affect the bone making process due to being expressed in high amounts in osteoblasts.

The phosphorylation of caldesmon and calponin by various kinases is suspected to play a role in smooth muscle contraction.

Human genes encoding calponin homology domain-containing proteins include:

Calponin tonically inhibits the ATPase activity of myosin in smooth muscle.

Fimbrin belongs to the calponin homology (CH) domain superfamily of actin cross-linking proteins.

Calponin is responsible for binding many actin binding proteins, phospholipids, and regulates the actin/myosin interaction.

Many actin-binding proteins, including α-actinin, β-spectrin, dystrophin, utrophin and fimbrin, do this through the actin-binding calponin homology domain.

Microtubule-associated monoxygenase, calponin and LIM domain containing 3, also known as MICAL3, is a human gene.

Smooth muscle does not contain troponin, but does contain the thin filament protein tropomyosin and other notable proteins - caldesmon and calponin.

Leucine-rich repeat and calponin homology domain-containing protein 4 is a protein that in humans is encoded by the LRCH4 gene.

At the CH domain calponin binds to α-actin and filamin and binds to actin within the RD domain.

Calponin homology actin-binding domain (or CH domain) is a superfamily of actin binding domains found in both cytoskeletal proteins and signal transduction proteins.

In 2004 the exact crystal structure of this actin binding domain(ABD) was determined in mice and shown to be composed of two calponin homology(CH) domains.

In double immunostained sections, these SMA-negative cells were also negative for SM-MHC, WT-1, CD10, and calponin (Fig.

The protein contains four IQ domains, one calponin homology domain, one Ras-GAP domain and one WW domain.

Smooth muscle does not contain the protein troponin; instead calmodulin (which takes on the regulatory role in smooth muscle), caldesmon and calponin are significant proteins expressed within smooth muscle.

Phosphorylation of calponin by a protein kinase, which is dependent upon calcium binding to calmodulin, releases the calponin's inhibition of the smooth muscle ATPase.

These domains in order of appearance are Calponin Homology (CH), regulatory domain (RD), and Click-23, domain that contains the calponin repeats.

The tissue homogenization conditions [ 1 ] favor extraction of the major smooth muscle cell contractile proteins actin and myosin, and the thin filament-binding components caldesmon, calponin, and tropomyosin (TM).

Starting at the N-terminus (or front of the protein), IQGAP1 contains a calponin homology domain (CHD), which mediates actin-binding and binds calponin.