Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 14 May 1993:
Vol. 260. no. 5110, pp. 979 - 983
DOI: 10.1126/science.8493535
Prev | Table of Contents | Next

Articles

Science, Vol 260, Issue 5110, 979-983
Copyright © 1993 by American Association for the Advancement of Science

articles

Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains

RL Brady, EJ Dodson, GG Dodson, G Lange, SJ Davis, AF Williams, and AN Barclay

Department of Chemistry, University of York, United Kingdom.

The CD4 antigen is a membrane glycoprotein of T lymphocytes that interacts with major histocompatibility complex class II antigens and is also a receptor for the human immunodeficiency virus. the extracellular portion of CD4 is predicted to fold into four immunoglobulin-like domains. The crystal structure of the third and fourth domains of rat CD4 was solved at 2.8 angstrom resolution and shows that both domains have immunoglobulin folds. Domain 3, however, lacks the disulfide between the beta sheets; this results in an expansion of the domain. There is a difference of 30 degrees in the orientation between domains 3 and 4 when compared with domains 1 and 2. The two CD4 fragment structures provide a basis from which models of the overall receptor can be proposed. These models suggest an extended structure comprising two rigid portions joined by a short and possibly flexible linker region.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Crystal Structure of HAb18G/CD147: IMPLICATIONS FOR IMMUNOGLOBULIN SUPERFAMILY HOMOPHILIC ADHESION.
X.-L. Yu, T. Hu, J.-M. Du, J.-P. Ding, X.-M. Yang, J. Zhang, B. Yang, X. Shen, Z. Zhang, W.-D. Zhong, et al. (2008)
J. Biol. Chem. 283, 18056-18065
   Abstract »    Full Text »    PDF »
Conformational Rearrangement within the Soluble Domains of the CD4 Receptor Is Ligand-specific.
Ashish, I. J. Juncadella, R. Garg, C. D. Boone, J. Anguita, and J. K. Krueger (2008)
J. Biol. Chem. 283, 2761-2772
   Abstract »    Full Text »    PDF »
Evidence for a Domain-Swapped CD4 Dimer as the Coreceptor for Binding to Class II MHC..
A. Maekawa, B. Schmidt, B. Fazekas de St. Groth, Y.-H. Sanejouand, and P. J. Hogg (2006)
J. Immunol. 176, 6873-6878
   Abstract »    Full Text »    PDF »
CD4 Dimers Constitute the Functional Component Required for T Cell Activation.
M.-C. Moldovan, A. Yachou, K. Levesque, H. Wu, W. A. Hendrickson, E. A. Cohen, and R.-P. Sekaly (2002)
J. Immunol. 169, 6261-6268
   Abstract »    Full Text »    PDF »
Identification of a CD4 Domain Required for Interleukin-16 Binding and Lymphocyte Activation.
Y. Liu, W. W. Cruikshank, T. O'Loughlin, P. O'Reilly, D. M. Center, and H. Kornfeld (1999)
J. Biol. Chem. 274, 23387-23395
   Abstract »    Full Text »    PDF »
Cloning and Modeling of the First Nonmammalian CD4.
R. Koskinen, U. Lamminmaki, C. A. Tregaskes, J. Salomonsen, J. R. Young, and O. Vainio (1999)
J. Immunol. 162, 4115-4121
   Abstract »    Full Text »    PDF »
Profound Enhancement of T Cell Activation Mediated by the Interaction Between the TCR and the D3 Domain of CD4.
D. A. A. Vignali and K. M. Vignali (1999)
J. Immunol. 162, 1431-1439
   Abstract »    Full Text »    PDF »
Cutting Edge: Novel RNA Ligands Able to Bind CD4 Antigen and Inhibit CD4+ T Lymphocyte Function.
E. Kraus, W. James, and A. N. Barclay (1998)
J. Immunol. 160, 5209-5212
   Abstract »    Full Text »    PDF »
Interactions between Brain-derived Neurotrophic Factor and the TRKB Receptor. IDENTIFICATION OF TWO LIGAND BINDING DOMAINS IN SOLUBLE TRKB BY AFFINITY SEPARATION AND CHEMICAL CROSS-LINKING.
M. Haniu, S. Montestruque, E. J. Bures, J. Talvenheimo, R. Toso, S. Lewis-Sandy, A. A. Welcher, and M. F. Rohde (1997)
J. Biol. Chem. 272, 25296-25303
   Abstract »    Full Text »    PDF »
Kinetic and structural analysis of mutant CD4 receptors that are defective in HIV gp120 binding.
H. Wu, D. G. Myszka, S. W. Tendian, C. G. Brouillette, R. W. Sweet, I. M. Chaiken, and W. A. Hendrickson (1996)
PNAS 93, 15030-15035
   Abstract »    Full Text »    PDF »
Both Extracellular Immunoglobin-like Domains of CD80 Contain Residues Critical for Binding T Cell Surface Receptors CTLA-4 and CD28.
R. J. Peach, Jür. Bajorath, J. Naemura, G. Leytze, J. Greene, A. Aruffo, and P. S. Linsley (1995)
J. Biol. Chem. 270, 21181-21187
   Abstract »    Full Text »    PDF »
Analysis of the Binding Site on Intercellular Adhesion Molecule 3 for the Leukocyte Integrin Lymphocyte Function-associated Antigen 1.
C. L. Holness, P. A. Bates, A. J. Littler, C. D. Buckley, A. McDowall, D. Bossy, N. Hogg, and D. L. Simmons (1995)
J. Biol. Chem. 270, 877-884
   Abstract »    Full Text »    PDF »
Structural motifs for recognition and adhesion in members of the immunoglobulin superfamily.
C. Holness and D. Simmons (1994)
J. Cell Sci. 107, 2065-2070
   PDF »
Crystal structure of the human CD4 N-terminal two-domain fragment complexed to a class II MHC molecule.
J.-h. Wang, R. Meijers, Y. Xiong, J.-h. Liu, T. Sakihama, R. Zhang, A. Joachimiak, and E. L. Reinherz (2001)
PNAS 98, 10799-10804
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)