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

Mrosek, Michael; Meier, Sebastian; Ucurum-Fotiadis, Zöhre; von Castelmur, Eleonore; Hedbom, Erik; Lustig, Ariel; Grzesiek, Stephan; Labeit, Dietmar; Labeit, Siegfried; Mayans, Olga (2008). Structural analysis of B-Box 2 from MuRF1: identification of a novel self-association pattern in a RING-like fold. Biochemistry, 47(40), pp. 10722-30. Washington, D.C.: American Chemical Society 10.1021/bi800733z

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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.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Department of Head Organs and Neurology (DKNS) > Clinic of Craniomaxillofacial Surgery

UniBE Contributor:

Hedbom, Erik

ISSN:

0006-2960

ISBN:

18795805

Publisher:

American Chemical Society

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 15:05

Last Modified:

04 May 2014 23:20

Publisher DOI:

10.1021/bi800733z

PubMed ID:

18795805

Web of Science ID:

000259603600021

URI:

https://boris.unibe.ch/id/eprint/28146 (FactScience: 117584)

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