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Integral membrane proteins are a permanent part of a cell membrane and can either penetrate the membrane (transmembrane) or associate with one or the other side of a membrane (integral monotopic). Peripheral membrane proteins are transiently associated with the cell membrane.
Integral monotopic proteins are permanently attached to the cell membrane from one side. [5] Three-dimensional structures of the following integral monotopic proteins have been determined: prostaglandin H2 syntheses 1 and 2 (cyclooxygenases) lanosterol synthase and squalene-hopene cyclase; microsomal prostaglandin E synthase
While the topologies of bitopic and polytopic membrane proteins can be linked to their function, monotopic proteins' topologies have yet to inform any function of these unique proteins apart from commonly being found in pathways where several enzymes are localized in sequence within the membrane. Depiction of how a monotopic membrane protein ...
Alpha-helical proteins are present in the inner membranes of bacterial cells or the plasma membrane of eukaryotic cells, and sometimes in the bacterial outer membrane. [5] This is the major category of transmembrane proteins. In humans, 27% of all proteins have been estimated to be alpha-helical membrane proteins. [6]
A pump is a protein that hydrolyses ATP to transport a particular solute through a membrane, and in doing so, generating an electrochemical gradient membrane potential. This gradient is of interest as an indicator of the state of the cell through parameters such as the Nernst potential .
Lanosterol synthase is a two-domain monomeric protein [10] composed of two connected (α/α) barrel domains and three smaller β-structures. The enzyme active site is in the center of the protein, closed off by a constricted channel. Passage of the (S)-2,3-epoxysqualene substrate through the channel requires a change in protein conformation.
The alternative oxidase is an integral monotopic membrane protein that is tightly bound to the inner mitochondrial membrane from matrix side [18] The enzyme has been predicted to contain a coupled diiron center on the basis of a conserved sequence motif consisting of the proposed iron ligands, four glutamate and two histidine amino acid residues. [19]
5743 19225 Ensembl ENSG00000073756 ENSMUSG00000032487 UniProt P35354 Q05769 RefSeq (mRNA) NM_000963 NM_011198 RefSeq (protein) NP_000954 NP_035328 Location (UCSC) Chr 1: 186.67 – 186.68 Mb Chr 1: 149.98 – 149.98 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Cyclooxygenase-2 (COX-2), also known as prostaglandin-endoperoxide synthase 2 (HUGO PTGS2), is an enzyme that in humans is ...