Hinge region: This area controls the movement of the receptor to the nucleus.

The simplest form is the hinge region from IgG1.

Yes - The method allows for some flexibility within the structures being compared, such as movements around hinge regions.

The Hsp60 monomer has three distinct sections separated by two hinge regions.

This largely conserved structure is bi-lobal, connected by a short hinge region.

This region has been termed the hinge region.

In one subgroup, the missing C1 seems to be replaced by an extended hinge region, as shown in the image.

The flexibility of Calmodulin's hinged region allows the molecule to "wrap around" its target.

The D domain is a hinge region that connects the C and E domains.

Cleavage of immunoglobulin A molecules at certain Pro- bonds in the hinge region.

The protein structure includes an actin binding N terminal domain, 24 internal repeats and 2 hinge regions.

The 5' domain and the hinge region act as a pre-rRNA-binding domain.

The structure of the hinge regions gives each of the four IgG classes its unique biological profile.

Even though there is about 95% similarity between their Fc regions, the structure of the hinge regions is relatively different.

A small hinge region between the DBD and LBD.

This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor.

Thus, the IgA protease act by cleaving the proline-rich hinge region of the heavy chain of IgA1.

To produce an F(ab')2 fragment, IgG is digested with pepsin, which cleaves the heavy chains near the hinge region.

Structurally, it is composed of three distinct regions: an N-terminal protein domain, a hinge region and a C-terminal cystein-rich domain.

The LAP complex contains a protease-sensitive hinge region which can be the potential target for this liberation of TGF-β.

The enzyme pepsin cleaves below hinge region, so a F(ab') fragment and a pFc' fragment is formed.

PKC-zeta has an N-terminal regulatory domain, followed by a hinge region and a C-terminal catalytic domain.

The protein has a transactivation domain linked by a relatively unstructured hinge region to a well-characterized DNA binding domain.

The structure of all PKCs consists of a regulatory domain and a catalytic domain tethered together by a hinge region.

Structurally hemopexin consists of two similar halves of approximately two hundred amino acid residues connected by a histidine-rich hinge region.