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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDEV6 |
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![]() | KRAB-associated protein 1 (KAP1); TRIM28; full length protein
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Function / homology | ![]() convergent extension involved in axis elongation / : / Krueppel-associated box domain binding / embryonic placenta morphogenesis / positive regulation of DNA methylation-dependent heterochromatin formation / suppression of viral release by host / epigenetic programming of gene expression / negative regulation of single stranded viral RNA replication via double stranded DNA intermediate / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function |
Biological species | ![]() ![]() |
![]() | ![]() Title: KAP1 is an antiparallel dimer with a functional asymmetry. Authors: Giulia Fonti / Maria J Marcaida / Louise C Bryan / Sylvain Träger / Alexandra S Kalantzi / Pierre-Yves Jl Helleboid / Davide Demurtas / Mark D Tully / Sergei Grudinin / Didier Trono / Beat ...Authors: Giulia Fonti / Maria J Marcaida / Louise C Bryan / Sylvain Träger / Alexandra S Kalantzi / Pierre-Yves Jl Helleboid / Davide Demurtas / Mark D Tully / Sergei Grudinin / Didier Trono / Beat Fierz / Matteo Dal Peraro / ![]() ![]() Abstract: KAP1 (KRAB domain-associated protein 1) plays a fundamental role in regulating gene expression in mammalian cells by recruiting different transcription factors and altering the chromatin state. In ...KAP1 (KRAB domain-associated protein 1) plays a fundamental role in regulating gene expression in mammalian cells by recruiting different transcription factors and altering the chromatin state. In doing so, KAP1 acts both as a platform for macromolecular interactions and as an E3 small ubiquitin modifier ligase. This work sheds light on the overall organization of the full-length protein combining solution scattering data, integrative modeling, and single-molecule experiments. We show that KAP1 is an elongated antiparallel dimer with an asymmetry at the C-terminal domains. This conformation is consistent with the finding that the Really Interesting New Gene (RING) domain contributes to KAP1 auto-SUMOylation. Importantly, this intrinsic asymmetry has key functional implications for the KAP1 network of interactions, as the heterochromatin protein 1 (HP1) occupies only one of the two putative HP1 binding sites on the KAP1 dimer, resulting in an unexpected stoichiometry, even in the context of chromatin fibers. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Related structure data | C: citing same article ( |
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Similar structure data |
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External links
Related items in Molecule of the Month |
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-Models
Model #2557 | ![]() Type: dummy / Radius of dummy atoms: 1.90 A / Symmetry ![]() ![]() |
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Model #2558 | ![]() Type: atomic / Symmetry ![]() ![]() |
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Sample
![]() | Name: KRAB-associated protein 1 (KAP1); TRIM28; full length protein Specimen concentration: 15 mg/ml |
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Buffer | Name: 20 mM HEPES, 500 mM NaCl, 10 % Glycerol, 2 mM TCEP / pH: 7.5 |
Entity #1350 | Name: KAP1FL / Type: protein Description: Transcription intermediary factor 1-beta, TIF1b, KAP1, TRIM28 Formula weight: 91.542 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: Q13263 Sequence: MGSSHHHHHH SQDPNSSSEN LYFQGAAASA AAASAAAASA AAASAGSPGP GEGSAGGEKR STAPSAAASA SASAAASSPA GGGAEALELL EHCGVCRERL RPEREPRLLP CLHSACSACL GPAAPAAANS SGDGGAAGDG TVVDCPVCKQ QCFSKDIVEN YFMRDSGSKA ...Sequence: MGSSHHHHHH SQDPNSSSEN LYFQGAAASA AAASAAAASA AAASAGSPGP GEGSAGGEKR STAPSAAASA SASAAASSPA GGGAEALELL EHCGVCRERL RPEREPRLLP CLHSACSACL GPAAPAAANS SGDGGAAGDG TVVDCPVCKQ QCFSKDIVEN YFMRDSGSKA ATDAQDANQC CTSCEDNAPA TSYCVECSEP LCETCVEAHQ RVKYTKDHTV RSTGPAKSRD GERTVYCNVH KHEPLVLFCE SCDTLTCRDC QLNAHKDHQY QFLEDAVRNQ RKLLASLVKR LGDKHATLQK STKEVRSSIR QVSDVQKRVQ VDVKMAILQI MKELNKRGRV LVNDAQKVTE GQQERLERQH WTMTKIQKHQ EHILRFASWA LESDNNTALL LSKKLIYFQL HRALKMIVDP VEPHGEMKFQ WDLNAWTKSA EAFGKIVAER PGTNSTGPAP MAPPRAPGPL SKQGSGSSQP MEVQEGYGFG SGDDPYSSAE PHVSGVKRSR SGEGEVSGLM RKVPRVSLER LDLDLTADSQ PPVFKVFPGS TTEDYNLIVI ERGAAAAATG QPGTAPAGTP GAPPLAGMAI VKEEETEAAI GAPPTATEGP ETKPVLMALA EGPGAEGPRL ASPSGSTSSG LEVVAPEGTS APGGGPGTLD DSATICRVCQ KPGDLVMCNQ CEFCFHLDCH LPALQDVPGE EWSCSLCHVL PDLKEEDGSL SLDGADSTGV VAKLSPANQR KCERVLLALF CHEPCRPLHQ LATDSTFSLD QPGGTLDLTL IRARLQEKLS PPYSSPQEFA QDVGRMFKQF NKLTEDKADV QSIIGLQRFF ETRMNEAFGD TKFSAVLVEP PPMSLPGAGL SSQELSGGPG DGP |
-Experimental information
Beam | Instrument name: ESRF BM29 / City: Grenoble / 国: France ![]() ![]() | ||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm | ||||||||||||||||||||||||||||||
Scan | Measurement date: Jul 6, 2017 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Unit: 1/nm /
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Distance distribution function P(R) |
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Result |
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