NationMaster - Encyclopedia: Pleckstrin homology domain

Pleckstrin homology domain (PH domain) is a protein region of approximately 120 amino acids that can bind Phosphatidylinositol lipids within biological membranes (such as Phosphatidylinositol (3,4,5)-trisphosphate and phosphatidylinositol (4,5)-bisphosphate), and proteins such as the βγ-subunits of heterotrimeric G proteins and protein kinase C. Through these interactions, PH domains play a role in recruiting proteins to different membranes, thus targeting them to appropriate cellular compartment or enabling them to interact with other components of the signal transduction pathways. A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... Phenylalanine is one of the standard amino acids. ... Chemical structure of sn-1-stearoyl-2-arachidonoyl phosphatidylinositol Phosphatidylinositol (abbreviated PtdIns, or PI) is a minor phospholipid component of eukaryotic cell membranes. ... Chemical structure of sn-1-stearoyl-2-arachidonoyl phosphatidylinositol 3,4,5-trisphosphate Phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3) commonly abbreviated to PIP3 is the product of the class I phosphoinositide 3-kinases (PI 3-kinases) activity on Phosphatidylinositol (4,5)-bisphosphate. ... Chemical structure of sn-1-stearoyl-2-arachidonoyl phosphatidylinositol 4,5-bisphosphate Phosphatidylinositol (4,5)-bisphosphate (PtdIns(4,5)P2) is a minor phospholipid component of cell membranes. ... G-proteins, short for guanine nucleotide binding proteins, are a family of proteins involved in second messenger cascades. ... A protein kinase is an enzyme that can transfer a phosphate group from a donor molecule (usually ATP) to an amino acid residue of a protein. ... The cell membrane (also called the plasma membrane, plasmalemma or phospholipid bilayer) is a semipermeable lipid bilayer common to all living cells. ... Cellular redirects here. ... In heraldry, a compartment is a design placed under the shield, usually rocks, a grassy mount, or some sort of other landscape upon which the supporters are depicted as standing (a compartment without supporters is possible but practically unknown, with the exception of South Australia[1]). It is sometimes said... It has been suggested that this article or section be merged with Signal transduction. ...

Individual PH domains possess specificities for phosphoinositides phosphorylated at different sites within the inositol ring, ie some bind phosphatidylinositol (4,5)-bisphosphate but not Phosphatidylinositol (3,4,5)-trisphosphate or Phosphatidylinositol (3,4)-bisphosphate or vice versa. This is important because it makes the recruitment of different PH domain containing proteins sensitive to the activities of enzymes that either phosphorylate or dephosphorylate these sites on the inositol ring, such as phosphoinositide 3-kinase or PTEN, respectively. Thus, such enzymes exert a part of their effect on cell function by modulating the localization of downstream signaling proteins that possess PH domains that are capable of binding their phospho-lipid products. Inositol, (of which the most prominent naturally-ocurring form is myo-inositol, cis-1,2,3,5-trans-4,6-cyclohexanehexol), is a carbocyclic polyol that plays an important role as the structural basis for a number of secondary messengers in eukaryotic cells, including inositol phosphates, phosphatidylinositol (PI) and phosphatidylinositol... Chemical structure of sn-1-stearoyl-2-arachidonoyl phosphatidylinositol (3,4)-bisphosphate Phosphatidylinositol (3,4)-bisphosphate (PtdIns(3,4)P2) is a minor phospholipid component of cell membranes, it is however an important second messenger. ... Phosphoinositide 3-kinases (PI 3-kinases or PI3Ks) are a family of related enzymes that are capable of phosphorylating the 3 position hydroxyl group of the inositol ring of phosphatidylinositol (PtdIns)[1]. The various 3-phosphorylated phosphoinositides that are produced by PI 3-kinases (PtdIns3P, PtdIns(3,4)P2, PtdIns... PTEN may mean: PTEN gene - one of the tumor suppressor gene (chromosome 10) Prime Time Entertainment Network ...

The unrelated FYVE domain binds Phosphatidylinositol 3-phosphate and has been found in over 60 proteins. FYVE zinc finger domain is named after four proteins that it has been found in: Fab1, YOTB/ZK632. ... Chemical structure of sn-1-stearoyl-2-arachidonoyl phosphatidylinositol 3-phosphate Phosphatidylinositol 3-phosphate (PtdIns3P) is the product of both the class II and III phosphoinositide 3-kinases (PI 3-kinases) activity on Phosphatidylinositol. ...

Other interactions

PH domains can also bind to other proteins, for example the PH domain of OSBP to ARF. Recruitment to the Golgi in this case is dependent on both PtdIns and ARF. A large number of PH domains have poor affinity for phosphoinositides and are hypothesized to function as protein binding domains. ADP Ribosylation Factors (ARFs) are members of the ARF family of GTP-binding proteins of the Ras superfamily. ...

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Protein domains

BZIP - DED - Kringle - PH - SH2 - SH3 - zinc finger - coiled coil - helix bundle - globin fold - twisted open sheet - alpha/beta barrels - up and down barrel - greek key barrel - jelly roll barrel - greek key - leucine-rich repeat - beta propeller - LIM domain - C2 domain A peripheral protein from the OPM database (P40phox PX domain of of NADPH oxidase). ... Within a protein, a structural domain (domain) is an element of overall structure that is self-stabilizing and often folds independently of the rest of the protein chain. ... Basic Leucine zipper domain (bZIP domain) CREB (top) is a transcription factor capable of binding DNAvia the bZIP domain (bottom) and regulating gene expression. ... The death-effector domain (DED) is a protein interaction domain found in inactive procaspases (cysteine proteases) and proteins that regulate caspase activation in the apoptosis cascade such as FAS-associating death domain-containing protein (FADD). ... Kringle Domains are conserved sequences that fold into large loops stabilized by 3 disulfide linkages. ... Ribbon diagram of the SH2 domain of human P56-Lck tyrosine kinase (PDB accession code 1LKK, chain A), colored from blue (N-terminus) to red (C-terminus). ... An SH3 domain is a protein module, a characteristic peptide sequence. ... Cartoon representation of the protein Zif268 (blue) containing three zinc fingers in complex with DNA (orange). ... A coiled coil is a structural motif found in many proteins. ... A helix bundle is a small protein fold composed of three or four alpha helices and held together by nonlocal hydrophobic interactions. ... An example of the globin fold, the oxygen-carrying protein myoglobin (PDB ID 1MBA) from the mollusc Aplysia limacina. ... Top view of a triosephosphateisomerase (TIM) barrel (PDB accession code 8TIM), colored from blue (N-terminus) to red (C-terminus). ... A simple Greek key design A Greek Key is a repeating design element used in architecture, jewelry and fabrics. ... An example of a leucine-rich repeat protein, a porcine ribonuclease inhibitor (PDB ID 2BNH). ... Ribbon diagram of the C-terminal WD40 domain of Tup1 (a transcriptional co-repressor in yeast), which adopts a 7-bladed beta-propeller fold. ... Structure of the 4th LIM of PINCH. Zinc atoms are shown in grey. ... The C2-domain of Î±-toxin (PDB 1OLP). ...

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