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PDBsum entry 4bmj
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62 a.a.
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66 a.a.
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58 a.a.
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59 a.a.
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PDB id:
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Apoptosis
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Title:
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Structure of the ubz1and2 tandem of the ubiquitin-binding adaptor protein tax1bp1
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Structure:
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Tax1-binding protein 1. Chain: a, b, c, d, e, f, g, h, i, j, k. Fragment: residues 725-789. Synonym: traf6-binding protein, tax1bp1. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta plyss.
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Resolution:
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2.75Å
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R-factor:
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0.217
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R-free:
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0.255
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Authors:
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M.A.Ceregido,M.Spinola-Amilibia,L.Buts,J.Rivera,J.Bravo,N.A.J.Van Nuland
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Key ref:
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M.A.Ceregido
et al.
(2014).
The structure of TAX1BP1 UBZ1+2 provides insight into target specificity and adaptability.
J Mol Biol,
426,
674-690.
PubMed id:
DOI:
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Date:
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09-May-13
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Release date:
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20-Nov-13
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PROCHECK
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Headers
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References
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Q86VP1
(TAXB1_HUMAN) -
Tax1-binding protein 1 from Homo sapiens
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Seq: Struc:
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789 a.a.
62 a.a.*
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Q86VP1
(TAXB1_HUMAN) -
Tax1-binding protein 1 from Homo sapiens
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Seq: Struc:
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789 a.a.
66 a.a.*
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Enzyme class:
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Chains A, B, C, D, E, F, G, H, I, J, K:
E.C.?
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DOI no:
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J Mol Biol
426:674-690
(2014)
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PubMed id:
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The structure of TAX1BP1 UBZ1+2 provides insight into target specificity and adaptability.
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M.A.Ceregido,
M.Spínola Amilibia,
L.Buts,
J.Rivera-Torres,
A.Garcia-Pino,
J.Bravo,
N.A.van Nuland.
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ABSTRACT
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TAX1BP1 is a novel ubiquitin-binding adaptor protein involved in the negative
regulation of the NF-kappaB transcription factor, which is a key player in
inflammatory responses, immunity and tumorigenesis. TAX1BP1 recruits A20 to the
ubiquitinated signaling proteins TRAF6 and RIP1, leading to their A20-mediated
deubiquitination and the disruption of IL-1-induced and TNF-induced NF-kappaB
signaling, respectively. The two zinc fingers localized at its C-terminus
function as novel ubiquitin-binding domains (UBZ, ubiquitin-binding zinc
finger). Here we present for the first time both the solution and crystal
structures of two classical UBZ domains in tandem within the human TAX1BP1. The
relative orientation of the two domains is slightly different in the X-ray
structure with respect to the NMR structure, indicating some degree of
conformational flexibility, which is rationalized by NMR relaxation data. The
observed degree of flexibility and stability between the two UBZ domains might
have consequences on the recognition mechanism of interacting partners.
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');
}
}
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