Dimeric association and segmental variability in the structure of human CD4
Identifieur interne : 003C76 ( Main/Exploration ); précédent : 003C75; suivant : 003C77Dimeric association and segmental variability in the structure of human CD4
Auteurs : Hao Wu [États-Unis] ; Peter D. Kwong [États-Unis] ; Wayne A. HendricksonSource :
- Nature [ 0028-0836 ] ; 1997-05-29.
Abstract
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 itscytoplasmic association with the lymphocyte kinase Lck (ref. 1). CD4 also serves as the high-affinity receptor for cellular attachment and entry of the human immunodeficiency virus (HIV)2. The extracellular portion of CD4 comprises four immunoglobulin-like domains (D1D4). This part of human CD4 (residues 1369) has been characterized as arecom-binant soluble protein (sCD4)3,4, and crystal structures have been described for the human D1D2 fragment5,6 and for the rat D3D4 fragment7. 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 importantin 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 may have relevance as mediators of signal transduction hi T cells.
Url:
DOI: 10.1038/387527a0
Affiliations:
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Hendrickson</name></author></analytic><monogr></monogr><series><title level="j" type="main">Nature</title><imprint><publisher>Nature Publishing Group</publisher><date when="1997-05-29">1997-05-29</date><biblScope unit="vol">387</biblScope><biblScope unit="issue">6632</biblScope><biblScope unit="page" from="527">527</biblScope><biblScope unit="page" to="530">530</biblScope><date type="Copyright" when="1997">1997</date></imprint><idno type="ISSN">0028-0836</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0028-0836</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">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 itscytoplasmic association with the lymphocyte kinase Lck (ref. 1). CD4 also serves as the high-affinity receptor for cellular attachment and entry of the human immunodeficiency virus (HIV)2. The extracellular portion of CD4 comprises four immunoglobulin-like domains (D1D4). This part of human CD4 (residues 1369) has been characterized as arecom-binant soluble protein (sCD4)3,4, and crystal structures have been described for the human D1D2 fragment5,6 and for the rat D3D4 fragment7. 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 importantin 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 may have relevance as mediators of signal transduction hi T cells.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region><settlement><li>New York</li></settlement><orgName><li>Université Columbia</li></orgName></list><tree><noCountry><name sortKey="Hendrickson, Wayne A" sort="Hendrickson, Wayne A" uniqKey="Hendrickson W" first="Wayne A." last="Hendrickson">Wayne A. Hendrickson</name></noCountry><country name="États-Unis"><region name="État de New York"><name sortKey="Wu, Hao" sort="Wu, Hao" uniqKey="Wu H" first="Hao" last="Wu">Hao Wu</name></region><name sortKey="Kwong, Peter D" sort="Kwong, Peter D" uniqKey="Kwong P" first="Peter D." last="Kwong">Peter D. Kwong</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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