ABCB3 p.Ser145Ala
| Predicted by SNAP2: | A: N (87%), C: N (93%), D: N (78%), E: N (72%), F: N (93%), G: N (87%), H: N (82%), I: N (87%), K: N (78%), L: N (87%), M: N (87%), N: N (87%), P: N (78%), Q: N (78%), R: N (78%), T: N (93%), V: N (87%), W: N (72%), Y: N (93%), |
| Predicted by PROVEAN: | A: N, C: N, D: D, E: N, F: N, G: D, H: N, I: D, K: N, L: D, M: N, N: N, P: D, Q: N, R: D, T: N, V: D, W: D, Y: N, |
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[hide] Structure of the human GINS complex and its assemb... Nat Struct Mol Biol. 2007 May;14(5):388-96. Epub 2007 Apr 8. Kamada K, Kubota Y, Arata T, Shindo Y, Hanaoka F
Structure of the human GINS complex and its assembly and functional interface in replication initiation.
Nat Struct Mol Biol. 2007 May;14(5):388-96. Epub 2007 Apr 8., [PMID:17417653]
Abstract [show]
The eukaryotic GINS complex is essential for the establishment of DNA replication forks and replisome progression. We report the crystal structure of the human GINS complex. The heterotetrameric complex adopts a pseudo symmetrical layered structure comprising two heterodimers, creating four subunit-subunit interfaces. The subunit structures of the heterodimers consist of two alternating domains. The C-terminal domains of the Sld5 and Psf1 subunits are connected by linker regions to the core complex, and the C-terminal domain of Sld5 is important for core complex assembly. In contrast, the C-terminal domain of Psf1 does not contribute to the stability of the complex but is crucial for chromatin binding and replication activity. These data suggest that the core complex ensures a stable platform for the C-terminal domain of Psf1 to act as a key interaction interface for other proteins in the replication-initiation process.
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151 (d) Chromatin-bound fractions in Xenopus GINS extracts immunodepleted by Xenopus Psf2 antibody, without sperm (lane 1) and with sperm (lanes 2-10), supplemented with 0.76 mM recombinant human GINS complex (lanes 1 and 2) or one of the following mutant complexes: domain deletion mutant GINS1Dc2 (lane 3) or GINS5Dc (lane 4); site-directed mutant GINS1Y147A (lane 5) or GINS1F176A (lane 6); or linker mutant GINS1-1 (L134A D135A I136A; lane 7), GINS1-2 (T137A Q138A D139A; lane 8), GINS1-3 (M140A K141A P142A; lane 9) or GINS1-4 (P143A K144A S145A; lane 10).
X
ABCB3 p.Ser145Ala 17417653:151:541
status: NEW