词条 | Kelch protein |
释义 |
| Symbol = Kelch_1 | Name = Kelch motif | image =1gof_front.GIF | width = | caption = | Pfam= PF01344 | InterPro= IPR006652 | SMART= | Prosite = | SCOP = 1gof | TCDB = | OPM family= | OPM protein= | PDB={{PDB3|1u6d}}X:459–504 {{PDB3|1zgk}}A:459–504 {{PDB3|1goh}} :311–357{{PDB3|1gof}} :311–357 {{PDB3|1gog}} :311–357 }} Kelch proteins (and Kelch-like proteins) are a widespread group of proteins that contain multiple Kelch motifs. The kelch domain generally occurs as a set of five to seven kelch tandem repeats that form a β-propeller tertiary structure. Kelch-repeat β-propellers are generally involved in protein–protein interactions, though the large diversity of domain architectures and limited sequence identity between kelch motifs make characterisation of the kelch superfamily difficult. StructureThe N-terminus of several Kelch proteins contain other protein domains, including Discoidin, F-box, and Broad-complex, Tramtrack, Bric-a-Brac/Poxvirus and Zincfinger (BTB/POZ) domains. Kelch proteins may also only have a β-propeller architecture. The BTB domain of kelch proteins (if present) allows the formation of homo- or heterodimers that mediate protein–protein interactions. The C-terminus of Kelch proteins contains kelch repeats. Each kelch repeat is a sequence of 44–55 amino acids in length, usually occurring in clusters of 4 – 7 repeats. Each kelch repeat forms a "blade" of the β-propeller fold, consisting of a four-stranded antiparallel β-sheet secondary structure, arranged radially around a central axis, packed onto its adjoining repeats via hydrophobic contacts. Kelch-repeat β-propellers undergo a variety of binding interactions with other proteins, notably the actin filaments of a cell. FunctionKelch like proteins are known to act as substrate adaptors for Cullin 3 ubiquitin ligases. OrganismsThe first Kelch protein (from which this family derives its name) was isolated from Drosophila, in which Kelch-mutant females lay sterile, cup-shaped eggs;[1] "Kelch" is German for "chalice", or "cup". Kelch proteins have also been isolated in many other animals, plants, bacteria, fungi, and even virus (restricted to Poxviridae). Human proteins containing Kelch motifsATRN; ATRNL1; CCIN; ENC1; FBXO42; GAN; HCFC1; HCFC2; IPP; IVNS1ABP; KBTBD10; KBTBD11; KBTBD2; KBTBD3; KBTBD4; KBTBD5; KBTBD6; KBTBD7; KBTBD8; KEAP1; KIAA1900; KLHDC1; KLHDC2; KLHDC3; KLHDC4; KLHDC5; KLHDC6; KLHDC7A; KLHDC7B; KLHDC8A; KLHDC8B; KLHDC9; KLHDC10; KLHL1; KLHL10; KLHL11; KLHL12; KLHL13; KLHL14; KLHL15; KLHL17; KLHL18; KLHL2; KLHL20; KLHL21; KLHL22; KLHL23; KLHL24; KLHL25; KLHL26; KLHL28; KLHL29; KLHL3; KLHL30; KLHL31; KLHL32; KLHL34; KLHL4; KLHL40; KLHL5; KLHL6; KLHL7; KLHL8; KLHL9; LZTR1; MEGF8; MKLN1; RABEPK; SARCOSIN; References1. ^UNDERSTANDING THE FUNCTION OF ACTIN-BINDING PROTEINS THROUGH GENETIC ANALYSIS OF DROSOPHILA OOGENESIS, by Andrew M. Hudson and Lynn Cooley; in the Annual Review of Genetics, Vol. 36: 455–488 (Volume publication date December 2002); retrieved 12 December 2013 {{refbegin}}
1 : Kelch proteins |
随便看 |
|
开放百科全书收录14589846条英语、德语、日语等多语种百科知识,基本涵盖了大多数领域的百科知识,是一部内容自由、开放的电子版国际百科全书。