• PMID
  • This entry represents the peptidase domain found in a group of aspartic endopeptidases of fungal origin, including aspergillopepsin (MEROPS ientifier A01.016) [ PMID: 11418762 ], rhizopuspepsin (A01.012), endothiapepsin (A01.017) and penicillopepsin (A01.011) [ PMID: 339694 ]. (ebi.ac.uk)
  • All PTPases carry the highly conserved active site motif C(X)5R (PTP signature motif), employ a common catalytic mechanism, and share a similar core structure made of a central parallel beta-sheet with flanking alpha-helices containing a beta-loop-alpha-loop that encompasses the PTP signature motif [ PMID: 9646865 ]. (ebi.ac.uk)
  • PKBs contain an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain [ PMID: 9742206 ]. (ebi.ac.uk)
  • fragment
  • Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken. (ebi.ac.uk)
  • Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2. (ebi.ac.uk)
  • Since mutation of Leu 817 to Arg abolishes the catalytic activity, Leu 817 is likely located near the active site of guanylate cyclase-A. These results demonstrate that the carboxyl fragment of guanylate cyclase-A is an ideal system for studying the active site of guanylate cyclase-A. (ahajournals.org)
  • The smaller FAK fragment is termed "killer FAT" and becomes the domain associated with death signaling. (wikipedia.org)
  • Proteins
  • Although proteins of the PARP family are related through their PARP catalytic domain, they do not resemble each other outside of that region, but rather, they contain unique domains that distinguish them from each other and hint at their discrete functions. (ebi.ac.uk)
  • APOBEC3G (apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G) is a human enzyme encoded by the APOBEC3G gene that belongs to the APOBEC superfamily of proteins. (wikipedia.org)
  • centre
  • The second class shows a release of evolutionary constraint for the sites around the catalytic centre, which emphasises a difference in function from the first group. (ebi.ac.uk)
  • The polypeptide has a highly conserved modular organisation consisting of an N-terminal DNA-binding domain, a central regulating segment, and a C-terminal or F region accommodating the catalytic centre. (ebi.ac.uk)
  • motifs
  • The methyltransferases or methylases are classified into three groups (Groups α, β, and γ) based on the sequential order of certain 9 motifs and the Target Recognition Domain (TRD). (wikipedia.org)
  • Motifs IV-VIII play a role in the catalytic activity, while motifs 1-III and X play a role in binding of the cofactor. (wikipedia.org)
  • Its primary structure comprises several domain motifs. (wikipedia.org)
  • membrane-bindin
  • Exon 2 contains the junction of the membrane-binding domain and the catalytic domain of b5R, which shows that there are two forms of b5R: a soluble form and a membrane-bound form. (wikipedia.org)
  • The NH2-terminal structure of the membrane-binding domain is CH3(CH2)12-CO-Gly-Ala-Gln-Leu-Ser-Thr-Leu-Gly-His-Met-Val-Leu-Phe-Pro-Val-Trp-Phe-Leu-Tyr-Ser-Leu-Leu-Met-Lys. (wikipedia.org)
  • activity
  • This domain catalyses a demethylase activity with a preference for 3-methylthymidine. (ebi.ac.uk)
  • Following the sIII strand the sequence meets the 'S-shaped double loop' that is of primary importance for the peptide structure and catalytic activity (see further) as it extends to the cleft side "bulge", continuing to the only antiparallel β-strand sIV, which is prime importance for binding peptidic substrates or inhibitors by forming main chain hydrogen bond. (wikipedia.org)
  • cytochrome
  • Cytochrome b5 reductase is involved in the transfer of reducing equivalents from the physiological electron donor, NADH, via an FAD domain to the small molecules of cytochrome b5. (wikipedia.org)
  • receptor
  • However, when PCSK9 binds to the LDLR (through the EGF-A domain), PCSK9 prevents the conformational change of the receptor-ligand complex. (wikipedia.org)
  • site
  • The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. (ebi.ac.uk)
  • 3 4 However, although the catalytic domain of GC-A has been assigned to a 239-amino acid region, 4 the exact location of the active site (or the catalytic cavity) is still unknown. (ahajournals.org)
  • The major obstacle is that the catalytic domain of GC-A does not contain G-x-G-x-x-G, the diagnostic consensus sequence of the nucleotide binding site that interacts with the phosphate chain of the nucleotide. (ahajournals.org)
  • mainly
  • The PH domain functions mainly in the interaction of PDPK1 with phosphatidylinositol (3,4)-bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate which is important in localization and activation of some of membrane associated PDPK1's substrates including AKT. (wikipedia.org)
  • histone
  • Nucleosome formation is dependent on the positive charges of the H4 histones and the negative charge on the surface of H2A histone fold domains. (wikipedia.org)
  • inactive
  • Inactive single domain phosphatases can still specifically bind substrates, and protect again dephosphorylation, while the inactive domains of tandem phosphatases can be further subdivided into two classes. (ebi.ac.uk)
  • function
  • The function of the amino-terminal domain is less clear, but it has been shown to interact with the beta-1 integrin subunit in vitro and is thought to be involved in the transduction of signals from ECM-integrin clusters. (wikipedia.org)
  • role
  • The Catalytic Domain of MMP-1 is composed of five highly twisted β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing a total of five metal ions, three Ca2+ and two Zn2+, one of which with catalytic role. (wikipedia.org)