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词条 Kelch protein
释义

  1. Structure

  2. Function

  3. Organisms

  4. Human proteins containing Kelch motifs

  5. References

{{Use dmy dates|date=December 2016}}{{more footnotes|date=July 2014}}{{Pfam_box
| 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.

Structure

The 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.

Function

Kelch like proteins are known to act as substrate adaptors for Cullin 3 ubiquitin ligases.

Organisms

The 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 motifs

ATRN; 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;

References

1. ^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}}
  • {{cite journal | vauthors = Lo SC, Li X, Henzl MT, Beamer LJ, Hannink M | title = Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling | journal = The EMBO Journal | volume = 25 | issue = 15 | pages = 3605–17 | date = August 2006 | pmid = 16888629 | pmc = 1538563 | doi = 10.1038/sj.emboj.7601243 }}
  • {{cite journal | vauthors = Zollman S, Godt D, Privé GG, Couderc JL, Laski FA | title = The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 91 | issue = 22 | pages = 10717–21 | date = October 1994 | pmid = 7938017 | pmc = 45093 | doi = 10.1073/pnas.91.22.10717 }}
  • {{cite journal | vauthors = Adams J, Kelso R, Cooley L | title = The kelch repeat superfamily of proteins: propellers of cell function | journal = Trends in Cell Biology | volume = 10 | issue = 1 | pages = 17–24 | date = January 2000 | pmid = 10603472 | doi = 10.1016/S0962-8924(99)01673-6 }}
{{refend}}{{Protein tandem repeats}}

1 : Kelch proteins

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