These enzymes contain a conserved motif Asp / Asn-Pro-Pro-Tyr / Phe in their N-terminal section, this conserved region could be involved in substrate binding or in the catalytic activity.

The molecule folds into 2 domains, an N-terminal catalytic domain, which contains the catalytic and cofactor binding sites, and comprises a central 9-stranded beta-sheet, surrounded by 5 helices ; and a C-terminal DNA recognition domain, which is formed by 4 small beta-sheets and 8 alpha-helices.

Dinoflagellate luciferase is a multi-domain protein, consisting of an N-terminal domain, and three catalytic domains, each of which preceded by a helical bundle domain.

A loop serving as the binding site for SAM links the N-terminal and the C-terminal domains of the Dot1 catalytic domain.

Each PRMT has a unique N-terminal region and a catalytic core.

The removal of the N-terminal residues ( Helicase and, RecQ-Ct domains ) impairs both helicase and ATPase activity but has no effect on the binding ability of RecQ implying that the N-terminus functions as the catalytic end.

Mammalian MTHFR is composed of an N-terminal catalytic domain and a C-terminal regulatory domain.

The class C GPCRs are distinguished by their large N-terminal tail, which also contains a ligand-binding domain.

Ubiquitin-receptor proteins have an N-terminal ubiquitin-like ( UBL ) domain and one or more ubiquitin-associated ( UBA ) domains.

The critical event leading to the activation of p53 is the phosphorylation of its N-terminal domain.

The N-terminal transcriptional activation domain contains a large number of phosphorylation sites and can be considered as the primary target for protein kinases transducing stress signals.

Steroid receptors, on the other hand, may be repressive on gene expression when their transactivation domain is hidden ; activity can be enhanced by phosphorylation of serine residues at their N-terminal as a result of another signal transduction pathway, a process called crosstalk.

The N-terminal DNA binding domain ( labeled ) of lac repressor | lac repressor binds the its target DNA sequence ( gold ) in the major groove using a helix-turn-helix motif.

* an N-terminal HH-CC zinc-binding domain ( a three-helical bundle stabilised by coordination of a Zn ( II ) cation )

The New York Academy of Sciences corroborated the acceptance of these receptors stating that " Recent molecular biological studies have now identified strong candidates for umami receptors, including the heterodimer T1R1 / T1R3, and truncated type 1 and 4 metabotropic glutamate receptors missing most of the N-terminal extracellular domain ( taste-mGluR4 and truncated-mGluR1 ) and brain-mGluR4.

* Flavohaemoglobins ( FHb ): chimeric, with an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD / FAD-binding domain.

* Globin-coupled sensors: chimeric, with an N-terminal myoglobin-like domain and a C-terminal domain that resembles the cytoplasmic signalling domain of bacterial chemoreceptors.

* Protoglobin: a single domain globin found in archaea that is related to the N-terminal domain of globin-coupled sensors.

For example, it has been shown to interact with fibrin, heparin, tenascin, TNF-α, BMP-1, rotavirus NSP-4, and many fibronectin binding proteins from bacteria ( like FBP-A ; FBP-B on the N-terminal domain ).

Type II and III are anchored with a signal-anchor sequence, with type II being targeted to the ER lumen with its C-terminal domain, while type III have their N-terminal domains targeted to the ER lumen.

Type IV is subdivided into IV-A, with their N-terminal domains targeted to the cytosol and IV-B, with an N-terminal domain targeted to the lumen.

Researchers are trying to target the ligand-binding domain and N-terminal domain of androgen receptors.

Compared to the X-ray crystal structure, the C-terminal domain solution structure is similar while the EF hands of the N-terminal domain are considerably less open.

HDV recognizes its receptor via the N-terminal domain of the large hepatitis B surface antigen, HBsAg.

Simultaneously there is a C35 cysteine residue at the N-terminal of the C-linker region that can reach two C481 residues, making a favorable disulfide bond compared to a C481-C481 bond.

Ligands may also bind elsewhere, however, as is the case for bulkier ligands ( e. g., proteins or large peptides ), which instead interact with the extracellular loops, or, as illustrated by the class C metabotropic glutamate receptors ( mGluRs ), the N-terminal tail.

A preprotein is a form that contains a signal sequence ( an N-terminal signal peptide ) that specifies its insertion into or through membranes, i. e., targets them for secretion.

This forms the proalbumin after the signal peptide is cleaved, and a further processing to remove the N-terminal 6-residue propeptide yields the mature form of the protein.

Because the 20S particle's central channel is narrow and gated by the N-terminal tails of the α ring subunits, the substrates must be at least partially unfolded before they enter the core.

The N-terminal signal sequence of the protein is recognized by a signal recognition particle ( SRP ) while the protein is still being synthesized on the ribosome.

The presequence translocase23 ( TIM23 ) is localized to the mitochondial inner membrane and acts a pore forming protein which binds precursor proteins with its N-terminal.

This means that trypsin predominantly cleaves proteins at the carboxyl side ( or " C-terminal side ") of the amino acids lysine and arginine except when either is bound to a N-terminal proline., although large-scale mass spectrometry data suggest cleavage occurs even with proline.

As a consequence, methionine is incorporated into the N-terminal position of all proteins in eukaryotes and archaea during translation, although it is usually removed by post-translational modification.

After binding to the receptors reelin is internalized by endocytosis, and the N-terminal fragment of the protein is re-secreted.

The active site is situated in the N-terminal half of the sequence, which includes a conserved Pro-Trp dipeptide ; the tryptophan has been shown to be involved in the binding of substrate by the enzyme.

According to a meta-analysis comparing BNP and N-terminal pro-BNP ( NTproBNP ) in the diagnosis of heart failure, BNP is a better indicator for heart failure and left ventricular systolic dysfunction.

The N-terminal domain is composed of two β-sheets in an αβαβα structure and a β barrel.

The C-terminal domain is connected to the N-terminal domain by a flexible hinge, which can separate the two domains.

Protein sequence can be determined by Edman degradation, in which the N-terminal residues are hydrolyzed from the chain one at a time, derivatized, and then identified.

Upon glutamate-binding to an mGluR, the N-terminal tail undergoes a conformational change that leads to its interaction with the residues of the extracellular loops and TM domains.

This precursor contains an N-terminal signal peptide, spacer, secretin itself ( residues 28 – 54 ), and a 72-amino acid C-terminal peptide.

The Metridia longa secreted luciferase gene encodes a 24 kDa protein containing an N-terminal secretory signal peptide of 17 amino acid residues.

It is unusual because in humans it contains 10 Se-Cys residues, which are split into two domains, a longer N-terminal domain that contains 1 Se-Cys, and a shorter C-terminal domain that contains 9 Se-Cys.

There is an N-terminal Zn ++ binding domain ( residues 1-110 ) where a zinc ion is tetrahedrally coordinated between one histidine and three cysteine residues, which may play a role in recognizing ssDNA.

N-terminal amino groups of valine residues in the α-and β-chains of deoxyhemoglobin exist as carbamates.

In histone acetylation and deacetylation, histone proteins are acetylated and deacetylated on lysine residues in the N-terminal tail as part of gene regulation.

The DENV NS5 protein is a 900 residue peptide with a methyltransferase domain at its N-terminal end ( residues 1-296 ) and a RNA-dependent RNA polymerase ( RdRp ) at its C-terminal end ( residues 320 – 900 ).

Counting of residues always starts at the N-terminal end ( NH < sub > 2 </ sub >- group ), which is the end where the amino group is not involved in a peptide bond.

Each subunit is composed of a large and a small domain, as well as a third domain consisting of the N-terminal residues 3-14 ; these few residues form a strand, which links and stabilizes the two subunits of the dimer.

The newly-formed N-terminal residue ( residue 16 ) insert into a cleft where its α-amino group forms an ion pair with the aspartate near the active site serine, and results in the conformational rearrangement of other residues.

Other important regions of the N-terminal domain for catalysis includes an oxyanion hole ( Trp-55, Leu-133 ), a lid region ( residues 216-239 ), as well as a β5 loop ( residues 54-64 ).

These proteins are very small, containing only 33 and 32 amino acids respectively, though some additional residues can be added to the N-terminal portion of each which are then presented on the outside of the coat.

In the split-ubiquitin system, two integral membrane proteins to be studied are fused to two different ubiquitin moieties: a C-terminal ubiquitin moiety (" Cub ", residues 35 – 76 ) and an N-terminal ubiquitin moiety (" Nub ", residues 1 – 34 ).

It consists of 512 amino acids ( aa ) with four glycosylation sites at asparagine residues and has N-terminal signal sequence ( 20 aa ), oligomerization and fusion domains and hydrophobic transmembrane domain near the C-terminus ( 7 aa ).