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Structural analysis of B-Box 2 from MuRF1 : identification of a novel self-association pattern in a RING-like fold.

Mrosek, Michael (author)
Division of Structural Biology, Biozentrum, University of Basel, Basel, Switzerland
Meier, Sebastian (author)
Division of Structural Biology, Biozentrum, University of Basel, Basel, Switzerland
Ucurum-Fotiadis, Zöhre (author)
Division of Structural Biology, Biozentrum, University of Basel, Basel, Switzerland
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von Castelmur, Eleonore (author)
Division of Structural Biology, Biozentrum, University of Basel, Basel, Switzerland
Hedbom, Erik (author)
Division of Structural Biology, Biozentrum, University of Basel, Basel, Switzerland
Lustig, Ariel (author)
Division of Structural Biology, Biozentrum, University of Basel, Basel, Switzerland
Grzesiek, Stephan (author)
Division of Structural Biology, Biozentrum, University of Basel, Basel, Switzerland
Labeit, Dietmar (author)
Institut für Anästhesiologie and Operative Intensivmedizin, Universitätsklinikum Mannheim, Mannheim, Germany
Labeit, Siegfried (author)
Institut für Anästhesiologie and Operative Intensivmedizin, Universitätsklinikum Mannheim, Mannheim, Germany
Mayans, Olga (author)
Division of Structural Biology, Biozentrum, University of Basel, Basel, Switzerland; School of Biological Sciences, University of Liverpool, Crown Street, Liverpool, U.K.
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 (creator_code:org_t)
2008-09-17
2008
English.
In: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 47:40, s. 10722-10730
Related links:
https://urn.kb.se/re...
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https://doi.org/10.1...
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  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Subject headings

NATURVETENSKAP  -- Kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences (hsv//eng)

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ref (subject category)
art (subject category)

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