Premium
Solution structure of the human HSPC280 protein
Author(s) -
Lin Jinzhong,
Zhou Tao,
Wang Jinfeng
Publication year - 2011
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.548
Subject(s) - antiparallel (mathematics) , protein structure , helix (gastropod) , crystallography , chemistry , protein secondary structure , residue (chemistry) , protein superfamily , nuclear magnetic resonance spectroscopy , dna , biophysics , stereochemistry , biology , biochemistry , physics , gene , ecology , quantum mechanics , snail , magnetic field
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.