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PDBsum entry 3rs1
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Immune system
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PDB id
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3rs1
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PDB id:
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| Name: |
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Immune system
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Title:
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MousE C-type lectin-related protein clrg
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Structure:
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C-type lectin domain family 2 member i. Chain: a, b. Fragment: extracellular domain (unp residues 85-206). Synonym: c-type lectin-related protein dcl1, c-type lectin-related protein g, clr-g, lymphoid-derived c-type lectin-1, lcl-1, osteoclast inhibitory lectin-related protein 2, ocil-related protein 2. Engineered: yes. Mutation: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Strain: c57bl/6. Gene: clec2i, clrg, dcl1, ocilrp2. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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Authors:
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T.Skalova,J.Dohnalek,J.Duskova,A.Stepankova,T.Koval,J.Hasek, K.Kotynkova,O.Vanek,K.Bezouska
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Key ref:
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T.Skálová
et al.
(2012).
Mouse Clr-g, a ligand for NK cell activation receptor NKR-P1F: crystal structure and biophysical properties.
J Immunol,
189,
4881-4889.
PubMed id:
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Date:
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02-May-11
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Release date:
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02-May-12
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PROCHECK
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Headers
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References
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Q9WVF9
(CLC2I_MOUSE) -
C-type lectin domain family 2 member I from Mus musculus
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Seq:
Struc:
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217 a.a.
122 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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J Immunol
189:4881-4889
(2012)
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PubMed id:
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Mouse Clr-g, a ligand for NK cell activation receptor NKR-P1F: crystal structure and biophysical properties.
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T.Skálová,
K.Kotýnková,
J.Dušková,
J.Hašek,
T.Koval,
P.Kolenko,
P.Novák,
P.Man,
P.Hanč,
O.Vaněk,
K.Bezouška,
J.Dohnálek.
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ABSTRACT
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Interactions between C-type lectin-like NK cell receptors and their protein
ligands form one of the key recognition mechanisms of the innate immune system
that is involved in the elimination of cells that have been malignantly
transformed, virally infected, or stressed by chemotherapy or other factors. We
determined an x-ray structure for the extracellular domain of mouse C-type
lectin related (Clr) protein g, a ligand for the activation receptor NKR-P1F.
Clr-g forms dimers in the crystal structure resembling those of human CD69. This
newly reported structure, together with the previously determined structure of
mouse receptor NKR-P1A, allowed the modeling and calculations of electrostatic
profiles for other closely related receptors and ligands. Despite the high
similarity among Clr-g, Clr-b, and human CD69, these molecules have
fundamentally different electrostatics, with distinct polarization of Clr-g. The
electrostatic profile of NKR-P1F is complementary to that of Clr-g, which
suggests a plausible interaction mechanism based on contacts between surface
sites of opposite potential.
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Links
