1wip: Difference between revisions
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'''STRUCTURE OF T-CELL SURFACE GLYCOPROTEIN CD4, MONOCLINIC CRYSTAL FORM'''<br /> | '''STRUCTURE OF T-CELL SURFACE GLYCOPROTEIN CD4, MONOCLINIC CRYSTAL FORM'''<br /> | ||
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==Overview== | ==Overview== | ||
CD4 is a co-receptor in the cellular immune response. It increases the, avidity of association between a T cell and an antigen-presenting cell by, interacting with non-polymorphic portions of the complex between class II, major histocompatibility complex (MHC) and T-cell receptor (TCR), molecules, and it contributes directly to signal transduction through its, cytoplasmic association with the lymphocyte kinase Lck. CD4 also serves as, the high-affinity receptor for cellular attachment and entry of the human, immunodeficiency virus (HIV). The extracellular portion of CD4 comprises, four immunoglobulin-like domains (D1-D4). This part of human CD4 (residues, 1-369) has been characterized as a recombinant soluble protein (sCD4), and, crystal structures have been described for the human D1D2 fragment and for, the rat D3D4 fragment. We have now determined the structures of intact, sCD4 in three crystal lattices. These structures have a hinge-like, variability at the D1D2 to D3D4 junction that might be important in immune, recognition and HIV fusion, and a common dimeric association through D4, domains. Dynamic light scattering measurements and chemical crosslinking, of sCD4 corroborate dimerization at high protein concentration. We suggest, that such dimers mayhave relevance as mediators of signal transduction in, T cells. | CD4 is a co-receptor in the cellular immune response. It increases the, avidity of association between a T cell and an antigen-presenting cell by, interacting with non-polymorphic portions of the complex between class II, major histocompatibility complex (MHC) and T-cell receptor (TCR), molecules, and it contributes directly to signal transduction through its, cytoplasmic association with the lymphocyte kinase Lck. CD4 also serves as, the high-affinity receptor for cellular attachment and entry of the human, immunodeficiency virus (HIV). The extracellular portion of CD4 comprises, four immunoglobulin-like domains (D1-D4). This part of human CD4 (residues, 1-369) has been characterized as a recombinant soluble protein (sCD4), and, crystal structures have been described for the human D1D2 fragment and for, the rat D3D4 fragment. We have now determined the structures of intact, sCD4 in three crystal lattices. These structures have a hinge-like, variability at the D1D2 to D3D4 junction that might be important in immune, recognition and HIV fusion, and a common dimeric association through D4, domains. Dynamic light scattering measurements and chemical crosslinking, of sCD4 corroborate dimerization at high protein concentration. We suggest, that such dimers mayhave relevance as mediators of signal transduction in, T cells. | ||
==Disease== | |||
Known diseases associated with this structure: CD4 lymphocyte deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=186940 186940]], Lupus erythematosus, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=186940 186940]] | |||
==About this Structure== | ==About this Structure== | ||
1WIP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1WIP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WIP OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:07:09 2008'' | ||
Revision as of 18:07, 15 February 2008
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STRUCTURE OF T-CELL SURFACE GLYCOPROTEIN CD4, MONOCLINIC CRYSTAL FORM
OverviewOverview
CD4 is a co-receptor in the cellular immune response. It increases the, avidity of association between a T cell and an antigen-presenting cell by, interacting with non-polymorphic portions of the complex between class II, major histocompatibility complex (MHC) and T-cell receptor (TCR), molecules, and it contributes directly to signal transduction through its, cytoplasmic association with the lymphocyte kinase Lck. CD4 also serves as, the high-affinity receptor for cellular attachment and entry of the human, immunodeficiency virus (HIV). The extracellular portion of CD4 comprises, four immunoglobulin-like domains (D1-D4). This part of human CD4 (residues, 1-369) has been characterized as a recombinant soluble protein (sCD4), and, crystal structures have been described for the human D1D2 fragment and for, the rat D3D4 fragment. We have now determined the structures of intact, sCD4 in three crystal lattices. These structures have a hinge-like, variability at the D1D2 to D3D4 junction that might be important in immune, recognition and HIV fusion, and a common dimeric association through D4, domains. Dynamic light scattering measurements and chemical crosslinking, of sCD4 corroborate dimerization at high protein concentration. We suggest, that such dimers mayhave relevance as mediators of signal transduction in, T cells.
DiseaseDisease
Known diseases associated with this structure: CD4 lymphocyte deficiency OMIM:[186940], Lupus erythematosus, susceptibility to OMIM:[186940]
About this StructureAbout this Structure
1WIP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Dimeric association and segmental variability in the structure of human CD4., Wu H, Kwong PD, Hendrickson WA, Nature. 1997 May 29;387(6632):527-30. PMID:9168119
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