2M17

ubiquitin-like domain-containing C-terminal domain phosphatase (UBLCP1)

Summary for 2M17

• Entry DOI: 10.2210/pdb2m17/pdb
• NMR Information: BMRB: 18844
• Descriptor: Ubiquitin-like domain-containing CTD phosphatase 1 (1 entity in total)
• Functional Keywords: ubiquitin-like domain-containing c-terminal domain phosphatase (ublcp1), hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q8WVY7
• Total number of polymer chains: 1
• Total formula weight: 8995.68

Authors

Lee, W.,Yun, J. (deposition date: 2012-11-19, release date: 2013-06-05, Last modification date: 2024-11-20)

Primary citation

Yun, J.H.,Ko, S.,Lee, C.K.,Cheong, H.K.,Cheong, C.,Yoon, J.B.,Lee, W.
Solution Structure and Rpn1 Interaction of the UBL Domain of Human RNA Polymerase II C-Terminal Domain Phosphatase.
Plos One, 8:e62981-e62981, 2013

PubMed Abstract: The 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 β-strand (β3) and β3-α2 loop, instead of the canonical β4 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 β3-α2 loop is relatively rigid although it might have intrinsic dynamic profile. The positively charged residues of the β3-α2 loop are involved in interacting with the C-terminal leucine-rich repeat-like domain of Rpn1.

PubMed: 23667555
DOI: 10.1371/journal.pone.0062981

Experimental method

SOLUTION NMR