2l2o

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l2o OCA], [https://pdbe.org/2l2o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l2o RCSB], [https://www.ebi.ac.uk/pdbsum/2l2o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l2o ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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 alpha-helices and four antiparallel beta-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 beta3 and beta4 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.

Solution structure of the human HSPC280 protein.,Lin J, Zhou T, Wang J Protein Sci. 2011 Jan;20(1):216-23. PMID:21082705<ref>PMID:21082705</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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