2m17
ubiquitin-like domain-containing C-terminal domain phosphatase (UBLCP1)
Structural highlights
FunctionUBCP1_HUMAN Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome.[1] [2] Publication Abstract from PubMedThe ubiquitin-like modifier (UBL) domain of ubiquitin-like domain proteins (UDPs) interacts specifically with subunits of the 26 S proteasome. A novel UDP, ubiquitin-like domain-containing C-terminal domain phosphatase (UBLCP1), has been identified as an interacting partner of the 26 S proteasome. We determined the high-resolution solution structure of the UBL domain of human UBLCP1 by nuclear magnetic resonance spectroscopy. The UBL domain of hUBLCP1 has a unique beta-strand (beta3) and beta3-alpha2 loop, instead of the canonical beta4 observed in other UBL domains. The molecular topology and secondary structures are different from those of known UBL domains including that of fly UBLCP1. Data from backbone dynamics shows that the beta3-alpha2 loop is relatively rigid although it might have intrinsic dynamic profile. The positively charged residues of the beta3-alpha2 loop are involved in interacting with the C-terminal leucine-rich repeat-like domain of Rpn1. Solution Structure and Rpn1 Interaction of the UBL Domain of Human RNA Polymerase II C-Terminal Domain Phosphatase.,Yun JH, Ko S, Lee CK, Cheong HK, Cheong C, Yoon JB, Lee W PLoS One. 2013 May 7;8(5):e62981. doi: 10.1371/journal.pone.0062981. Print 2013. PMID:23667555[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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