2L2O

Solution structure of human HSPC280 protein

Summary for 2L2O

• Entry DOI: 10.2210/pdb2l2o/pdb
• Descriptor: UPF0727 protein C6orf115 (1 entity in total)
• Functional Keywords: hspc280, c6orf115, winged helix, unknown function
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 10125.58

Authors

Lin, J.,Wang, J. (deposition date: 2010-08-24, release date: 2011-07-06, Last modification date: 2024-05-01)

Primary citation

Lin, J.,Zhou, T.,Wang, J.
Solution structure of the human HSPC280 protein
Protein Sci., 20:216-223, 2011

PubMed Abstract: The human HSPC280 protein belongs to a new family of low molecular weight proteins, which is only present in eukaryotes, and is absent in fungi. The solution structure of HSPC280 was determined using multidimensional NMR spectroscopy. The overall structure consists of three α-helices and four antiparallel β-strands and has a winged helix-like fold. However, HEPC280 is not a typical DNA-binding winged helix protein in that it lacks DNA-binding activity. Unlike most winged-helix proteins, HSPC280 has an unusually long 13-residue (P62-V74) wing 1 loop connecting the β3 and β4 strands of the protein. Molecules of HSPC280 have a positively charged surface on one side and a negatively charged surface on the other side of the protein structure. Comparisons with the C-terminal 80-residue domain of proteins in the Abra family reveal a conserved hydrophobic groove in the HSPC280 family, which may allow HSPC280 to interact with other proteins.

PubMed: 21082705
DOI: 10.1002/pro.548

Experimental method

SOLUTION NMR