Biomolecular NMR Assignments

, Volume 10, Issue 1, pp 189–192 | Cite as

1H, 13C and 15N resonance assignments of human DCL-1 (CD302) extracellular domain

  • Eliška Pospíšilová
  • Daniel Kavan
  • Petr Novák
  • Josef Chmelík


DCL-1 (CD302) is a single-pass type one transmembrane protein which is predominantly expressed on myeloid cell lines. It possess the ability of endocytosis and is assumed to play a role in cell adhesion and migration. It has been also connected to several illnesses but more on the level of mRNA than on the protein expression level. More interestingly it is alternatively expressed in the form of a fusion protein with another single-pass type one transmembrane protein DEC205 (CD205) which is normally involved in antigen-uptake and endocytosis. The fusion protein has been assigned to have altered function compared to the wild type proteins. We have performed NMR structural analysis of the 16.2 kDa extracellular domain of DCL-1 to get a better insight onto this molecule. We have been able to assign nearly 97 % of resonance frequencies for the 15N and 13C labeled recombinant protein. The assignments have been deposited into Biological Magnetic Resonance Data Bank under the accession number 25802.


DCL-1 (CD302) C-type lectin like receptor Protein NMR Heteronuclear NMR spectroscopy Resonance assignment 



This work has been supported by the Institutional Research Concept of the Institute of Microbiology (RVO61388971); and grants from the Ministry of Education Youth and Sports of the Czech Republic (LO1509) and European Regional Development Funds (CZ.1.07/2.3.00/20.0055, CZ.1.07/2.3.00/30.0003 and CZ.1.05/1.1.00/02.0109); Charles University in Prague (GAUK 797213 and project UNCE 204025/2012); and the Czech Science Foundation (P207/10/1040). Access to instruments and other facilities was supported by the EU (Operational Program Prague—Competitiveness project CZ.2.16/3.1.00/24023).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.


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Copyright information

© Springer Science+Business Media Dordrecht 2016

Authors and Affiliations

  1. 1.Department of Biochemistry, Faculty of ScienceCharles University in PraguePragueCzech Republic
  2. 2.Institute of MicrobiologyAcademy of Sciences of the Czech RepublicPragueCzech Republic

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