Dimeric association and segmental virability in the structure of human CD4

Article Abstract:

CD4 acts as a co-receptor in the cellular immune response, increasing the avidity of links between T cells and antigen-presenting cells, through non-polymorphic interaction. CD4 also acts as a high affinity receptor for cell attachment and entry of HIV, the human immuno-deficiency virus. Recombinant soluble protein (sCD4) were grown, beginning from the selenomethionyl protein. Structures of intact sCD4 were determined in three crystal lattices, providing hinge like variability at D1D2 and D3D4 junctions, which could be significant in immune recognition and HIV fusion.

Cell receptors, CD4 lymphocytes

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The antigenic structure of the HIV gp120 envelope glycoprotein

Article Abstract:

Acquired immunodeficiency syndrome (AIDS) is caused by the human immunodeficiency virus HIV-1, whose entry into target cells is mediated by the HIV-1 envelope glycoproteins gp120 and gp41. Entry of the virus depends on interaction between target cell receptors and the gp120 exterior glycoprotein. A new study investigates the crystal structure of the gp120 surface glycoprotein. It is hoped that greater understanding of HIV-1's ability to penetrate the humoral immune response will help in vaccine design.

HIV (Viruses), HIV, Genetic aspects, Viral envelopes, AIDS (Disease), AIDS research

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Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation

Article Abstract:

The Src-family tyrosine kinase Lck is expressed in the T lymphocytes and includes SH3, SH2 and kinase domains. It performs tyrosine phosphorylation and is also influenced by it. The pTyr 505 present at the C-terminal end of the Lck bind with the SH2 domain. This, in turn, suppresses kinase activity. The intramolecular complex between the SH2 domain and the Lck tyrosine kinase is possible only when both the structures change their structures.

Analysis, Protein tyrosine kinase, Protein-tyrosine kinase, Phosphorylation, T cells

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