1ttn

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ttn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ttn OCA], [http://www.ebi.ac.uk/pdbsum/1ttn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ttn RCSB]</span>
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[[Category: ubiquitin-like domain]]
[[Category: ubiquitin-like domain]]
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Revision as of 21:00, 30 March 2008


PDB ID 1ttn

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Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Solution structure of the ubiquitin-like domain of human DC-UBP from dendritic cells


Overview

The previously identified dendritic cell-derived ubiquitin-like protein (DC-UbP) was implicated in cellular differentiation and apoptosis. Sequence alignment suggested that it contains a ubiquitin-like (UbL) domain in the C terminus. Here, we present the solution NMR structure and backbone dynamics of the UbL domain of DC-UbP. The overall structure of the domain is very similar to that of Ub despite low similarity (<30%) in amino-acid sequence. One distinct feature of the domain structure is its highly positively charged surface that is different from the corresponding surfaces of the well-known UbL modifiers, Ub, NEDD8, and SUMO-1. The key amino-acid residues responsible for guiding polyubiquitinated proteins to proteasome degradation in Ub are not conserved in the UbL domain. This implies that the UbL domain of DC-UbP may have its own specific interaction partners with other yet unknown cellular functions related to the Ub pathway.

About this Structure

1TTN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of the ubiquitin-like domain of human DC-UbP from dendritic cells., Gao YG, Song AX, Shi YH, Chang YG, Liu SX, Yu YZ, Cao XT, Lin DH, Hu HY, Protein Sci. 2005 Aug;14(8):2044-50. Epub 2005 Jun 29. PMID:15987890

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