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Structure paper

TitleFour crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 71, Page 578-591, Year 2015
Publish dateJun 6, 2014 (structure data deposition date)
AuthorsSkalova, T. / Blaha, J. / Harlos, K. / Duskova, J. / Koval, T. / Stransky, J. / Hasek, J. / Vanek, O. / Dohnalek, J.
External linksActa Crystallogr. ,Sect. D / PubMed:25760607
MethodsX-ray diffraction
Resolution1.8 - 2.75 Å
Structure data

PDB-4qkg:
Monomeric form of human LLT1, a ligand for NKR-P1
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-4qkh:
Dimeric form of human LLT1, a ligand for NKR-P1
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-4qki:
Dimeric form of human LLT1, a ligand for NKR-P1
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-4qkj:
Glycosylated form of human LLT1, a ligand for NKR-P1, in this structure forming hexamers
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

Chemicals

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / C-type lectin like fold / ligand for human receptor NKR-P1 / glycosylation; deglycosylated after the first GlcNac unit / anchored in membrane on cell surface / GlcNAc2Man5 glycosylation

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