Literature DB >> 20054122

The high-resolution structure of the extracellular domain of human CD69 using a novel polymer.

Petr Kolenko1, Tereza Skálová, Ondrej Vanek, Andrea Stepánková, Jarmila Dusková, Jindrich Hasek, Karel Bezouska, Jan Dohnálek.   

Abstract

The structure of the extracellular domain of human CD69 has been determined by single-crystal X-ray diffraction. The structure refined to 1.37 A resolution provides further details of the overall structure and the asymmetric interface between the monomers in the native dimer. The protein was crystallized using di[poly(ethylene glycol)] adipate, which also served as a cryoprotectant. This is the first report of a crystal structure determined using crystals grown with this polymer.

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Year:  2009        PMID： 20054122      PMCID： PMC2802874          DOI： 10.1107/S1744309109043152

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  16 in total

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6.  T cell activation via Leu-23 (CD69).

Authors:  R Testi; J H Phillips; L L Lanier
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Review 8.  Biology of animal lectins.

Authors:  K Drickamer; M E Taylor
Journal:  Annu Rev Cell Biol       Date:  1993

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10.  Multiple dimeric forms of human CD69 result from differential addition of N-glycans to typical (Asn-X-Ser/Thr) and atypical (Asn-X-cys) glycosylation motifs.

Authors:  B A Vance; W Wu; R K Ribaudo; D M Segal; K P Kearse
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2.  Characterization of alternatively spliced transcript variants of CLEC2D gene.

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4.  Proline/alanine-rich sequence (PAS) polypeptides as an alternative to PEG precipitants for protein crystallization.

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5.  Structure of the human NK cell NKR-P1:LLT1 receptor:ligand complex reveals clustering in the immune synapse.

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6.  Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states.

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  6 in total

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