3ddt

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Crystal structure of the B2 box from MuRF1 in dimeric stateCrystal structure of the B2 box from MuRF1 in dimeric state

Structural highlights

3ddt is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TRI63_HUMAN] E3 ubiquitin ligase. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The B-box motif is the defining feature of the TRIM family of proteins, characterized by a RING finger-B-box-coiled coil tripartite fold. We have elucidated the crystal structure of B-box 2 (B2) from MuRF1, a TRIM protein that supports a wide variety of protein interactions in the sarcomere and regulates the trophic state of striated muscle tissue. MuRF1 B2 coordinates two zinc ions through a cross-brace alpha/beta-topology typical of members of the RING finger superfamily. However, it self-associates into dimers with high affinity. The dimerization pattern is mediated by the helical component of this fold and is unique among RING-like folds. This B2 reveals a long shallow groove that encircles the C-terminal metal binding site ZnII and appears as the defining protein-protein interaction feature of this domain. A cluster of conserved hydrophobic residues in this groove and, in particular, a highly conserved aromatic residue (Y133 in MuRF1 B2) is likely to be central to this role. We expect these findings to aid the future exploration of the cellular function and therapeutic potential of MuRF1.

Structural analysis of B-Box 2 from MuRF1: identification of a novel self-association pattern in a RING-like fold.,Mrosek M, Meier S, Ucurum-Fotiadis Z, von Castelmur E, Hedbom E, Lustig A, Grzesiek S, Labeit D, Labeit S, Mayans O Biochemistry. 2008 Oct 7;47(40):10722-30. Epub 2008 Sep 17. PMID:18795805[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. McElhinny AS, Kakinuma K, Sorimachi H, Labeit S, Gregorio CC. Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1. J Cell Biol. 2002 Apr 1;157(1):125-36. Epub 2002 Apr 1. PMID:11927605 doi:http://dx.doi.org/10.1083/jcb.200108089
  2. Mrosek M, Meier S, Ucurum-Fotiadis Z, von Castelmur E, Hedbom E, Lustig A, Grzesiek S, Labeit D, Labeit S, Mayans O. Structural analysis of B-Box 2 from MuRF1: identification of a novel self-association pattern in a RING-like fold. Biochemistry. 2008 Oct 7;47(40):10722-30. Epub 2008 Sep 17. PMID:18795805 doi:10.1021/bi800733z

3ddt, resolution 1.90Å

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