Molecular architecture of mouse activating NKR-P1 receptors

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• 作者：Petr Kolenko^a ; ¹ ; Daniel Rozbeský ; ^b ; ^c ; ¹ ; Ond&#x159 ; ej Vaně ; k^b ; ^c ; Vladimí ; r Kopecký ; Jr.^d ; Kate&#x159 ; ina Hofbauerová ; ^c ; ^d ; Petr Nová ; k^c ; Petr Pompach^c ; Jind&#x159 ; ich Haš ; ek^a ; Tereza Ská ; lová ; ^a ; Karel Bezouš ; ka^b ; ^c ; Jan Dohná ; lek^a ; ^{dohnalek007@gmail.com"" rel=""nofollow}
• 关键词：NK cell ; C-type lectin-like receptor ; X-ray structure ; Receptor– ; ligand interaction
• 刊名：Journal of Structural Biology
• 出版年：2011
• 出版时间：September 2011
• 年：2011
• 卷：175
• 期：3
• 页码：434-441
• 全文大小：1135 K

文摘

Receptors belonging to NKR-P1 family and their specific Clr ligands form an alternative missing self recognition system critical in immunity against tumors and viruses, elimination of tumor cells subjected to genotoxic stress, activation of T cell dependent immune response, and hypertension. The three-dimensional structure of the extracellular domain of the mouse natural killer (NK) cell receptor mNKR-P1Aex has been determined by X-ray diffraction. The core of the C-type lectin domain (CTLD) is homologous to the other CTLD receptors whereas one quarter of the domain forms an extended loop interacting tightly with a neighboring loop in the crystal. This domain swapping mechanism results in a compact interaction interface. A second dimerization interface resembles the known arrangement of other CTLD NK receptors. A functional dimeric form of the receptor is suggested, with the loop, evolutionarily conserved within this family, proposed to participate in interactions with ligands.