WD40 ponavljanje
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| Trakasti dijagram C-terminalnog WD40 domena proteina Tup1 (transkripcionog korepresora kod kvasca), koji poprima oblik beta-propelera sa sedam lopatica. Traka je obojena od plavog N-terminusa do crvenog C-terminusa.[1] | |||||||||
| Identifikatori | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Simbol | WD40 | ||||||||
| Pfam | PF00400 | ||||||||
| Pfam klan | CL0186 | ||||||||
| InterPro | IPR001680 | ||||||||
| PROSITE | PDOC00574 | ||||||||
| SCOP | 1gp2 | ||||||||
| Superfamilija | 1gp2 | ||||||||
| CDD | cd00200 | ||||||||
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WD40 ponavljanje (WD, beta-transducinsko ponavljanje) je kratak strukturni motiv od aproksimativno 40 aminokiselina, koji se često završava sa dipeptidom triptofan-aspartinska kiselina (W-D).[2] Nekoliko ponavljanja ovog tipa se kombinuje da formira WD domen.
Struktura[uredi | uredi kod]
Proteini koji sadrže WD motiv imaju od 4 do 16 ponavljajućih jedinica, koje formiraju kružnu beta-propelersku strukturu.[3][4]
Funkcija[uredi | uredi kod]
Proteini sa WD ponavljanjem su velika familija, koja je prisutna kod svih eukariota. Oni su implicirani u raznovrsne funkcije u opsegu od prenosa signala i transkripcione regulacije do kontrole ćelijskog ciklusa, autofagije i apoptoze. Zajednička funkcija svih ovih proteina je koordinacija multiproteinskih kompleksa, pri čemu ponavljajuće jedinice služe kao kruta osnova za proteinske interakcije. Specifičnost proteina je određena sekvencama izvan samih ponavljanja. Primeri ovakvih kompleksa su G proteini (beta podjedinica je beta-propeler), TAFII transkripcioni faktor, i E3 ubikvitinska ligaza.[3][4]
Primeri[uredi | uredi kod]
Ljudski geni koji koriraju proteine sa ovim domenom su:
- AAAS, AAMP, AHI1, AMBRA1, APAF1, ARPC1A, ARPC1B, ATG16L1,
- BOP1, BRWD1, BRWD2, BRWD3, BTRC, BUB3,
- C6orf11, CDC20, CDC40, CDRT1, CHAF1B, CIAO1, CIRH1A, COPA, COPB2, CORO1A, CORO1B, CORO1C, CORO2A, CORO2B, CORO6, CORO7, CSTF1,
- DDB2, DENND3, DMWD, DMXL1, DMXL2, DNAI1, DNAI2, DNCI1, DTL, DYNC1I1, DYNC1I2, EDC4,
- EED, EIF3S2, ELP2, EML1, EML2, EML3, EML4, EML4-ALK, EML5, ERCC8,
- FBXW10, FBXW11, FBXW2, FBXW4, FBXW5, FBXW7, FBXW8, FBXW9, FZR1,
- GBL, GEMIN5, GNB1, GNB1L, GNB2, GNB2L1, GNB3, GNB4, GNB5, GRWD1, GTF3C2,
- HERC1, HIRA, HZGJ,
- IFT122, IFT140, IFT172, IFT80, IQWD1,
- KATNB1, KIAA1336, KIF21A, KIF21B, KM-PA-2,
- LLGL1, LLGL2, LRBA, LRRK1, LRRK2, LRWD1, LYST,
- MAPKBP1, MED16, MORG1,
- NBEA, NBEAL1, NEDD1, NLE1, NSMAF, NUP37, NUP43, NWD1,
- PAAF1, PAFAH1B1, PAK1IP1, PEX7, PHIP, PIK3R4, PLAA, PLRG1, PPP2R2B, PPP2R2C, PPWD1, PREB, PRPF19, PRPF4, PWP1, PWP2,
- RAE1, RAPTOR, RBBP4, RBBP5, RBBP7, RFWD2, RFWD3, RRP9,
- SCAP, SEC13, SEC31A, SEC31B, SEH1L, SHKBP1, SMU1, SPAG16, SPG, STRAP, STRN, STRN3, STRN4, STXBP5, STXBP5L,
- TAF5, TAF5L, TBL1X, TBL1XR1, TBL1Y, TBL2, TBL3, TEP1, THOC3, THOC6, TLE1, TLE2, TLE3, TLE4, TLE6, TRAF7, TSSC1, TULP4, TUWD12,
- UTP15, UTP18,
- WAIT1, WDF3, WDFY1, WDFY2, WDFY3, WDFY4, WDHD1, WDR1, WDR10, WDR12, WDR13, WDR16, WDR17, WDR18, WDR19, WDR20, WDR21A, WDR21C, WDR22, WDR23, WDR24, WDR25, WDR26, WDR27, WDR3, WDR31, WDR32, WDR33, WDR34, WDR35, WDR36, WDR37, WDR38, WDR4, WDR40A, WDR40B, WDR40C, WDR41, WDR42A, WDR42B, WDR43, WDR44, WDR46, WDR47, WDR48, WDR49, WDR5, WDR51A, WDR51B, WDR52, WDR53, WDR54, WDR55, WDR57, WDR59, WDR5B, WDR6, WDR60, WDR61, WDR62, WDR63, WDR64, WDR65, WDR66, WDR67, WDR68, WDR69, WDR7, WDR70, WDR72, WDR73, WDR74, WDR75, WDR76, WDR77, WDR78, WDR79, WDR8, WDR81, WDR82, WDR85, WDR86, WDR88, WDR89, WDR90, WDR91, WDR92, WDSOF1, WDSUB1, WDTC1, WSB1, WSB2,
- ZFP106
Reference[uredi | uredi kod]
- ↑ PDB 1erj; Sprague ER, Redd MJ, Johnson AD, Wolberger C (June 2000). „Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast”. EMBO J. 19 (12): 3016–27. DOI:10.1093/emboj/19.12.3016. PMC 203344. PMID 10856245.
- ↑ Neer EJ, Schmidt CJ, Nambudripad R, Smith TF (September 1994). „The ancient regulatory-protein family of WD-repeat proteins”. Nature 371 (6495): 297–300. DOI:10.1038/371297a0. PMID 8090199.
- ↑ 3,0 3,1 Smith TF, Gaitatzes C, Saxena K, Neer EJ (May 1999). „The WD repeat: a common architecture for diverse functions”. Trends Biochem. Sci. 24 (5): 181–5. DOI:10.1016/S0968-0004(99)01384-5. PMID 10322433.
- ↑ 4,0 4,1 Li D, Roberts R (December 2001). „WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases”. Cell. Mol. Life Sci. 58 (14): 2085–97. DOI:10.1007/PL00000838. PMID 11814058.
Spoljašnje veze[uredi | uredi kod]
- Eukaryotic Linear Motif resource motif class LIG_APCC_Dbox_1
- Eukaryotic Linear Motif resource motif class LIG_APCC_KENbox_2
- Eukaryotic Linear Motif resource motif class LIG_COP1
- Eukaryotic Linear Motif resource motif class LIG_EH1_1
- Eukaryotic Linear Motif resource motif class LIG_GLEBS_BUB3_1
- Eukaryotic Linear Motif resource motif class LIG_RAPTOR_TOS_1
- Eukaryotic Linear Motif resource motif class LIG_SCF_FBW7_1
- Eukaryotic Linear Motif resource motif class LIG_SCF_FBW7_2
- Eukaryotic Linear Motif resource motif class LIG_SCF-TrCP1_1
- Eukaryotic Linear Motif resource motif class LIG_WRPW_1
- Eukaryotic Linear Motif resource motif class LIG_WRPW_2
- Eukaryotic Linear Motif resource motif class TRG_Golgi_diPhe_1
- Eukaryotic Linear Motif resource motif class TRG_PTS2