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PDBsum entry 1hng
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T lymphocyte adhesion glycoprotein PDB id
1hng

 

 

 

 

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Contents
Protein chains
175 a.a. *
* Residue conservation analysis
PDB id:
1hng
Name: T lymphocyte adhesion glycoprotein
Title: Crystal structure at 2.8 angstroms resolution of a soluble form of the cell adhesion molecule cd2
Structure: Cd2. Chain: a, b. Engineered: yes
Source: Rattus rattus. Black rat. Organism_taxid: 10117. Organ: ovary
Biol. unit: Dimer (from PQS)
Resolution:
2.80Å     R-factor:   0.215    
Authors: E.Y.Jones,S.J.Davis,A.F.Williams,K.Harlos,D.I.Stuart
Key ref: E.Y.Jones et al. (1992). Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2. Nature, 360, 232-239. PubMed id: 1279440
Date:
10-Aug-94     Release date:   07-Feb-95    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P08921  (CD2_RAT) -  T-cell surface antigen CD2 from Rattus norvegicus
Seq:
Struc: 		344 a.a.
175 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Nature 360:232-239 (1992)
PubMed id: 1279440  
 
 
Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2.
E.Y.Jones, S.J.Davis, A.F.Williams, K.Harlos, D.I.Stuart.
 
  ABSTRACT  
 
The crystal structure of a soluble form of the T lymphocyte antigen CD2 provides the first complete view of the extracellular region of a cell adhesion molecule. The topology of the molecule, which comprises two immunoglobulin-like domains, is the same as that of the first two domains of CD4 but the relative domain orientation is altered by a fairly flexible linker region. The putative ligand-binding beta-sheet forms a flat surface towards the top of the molecule. Crystal contacts between these surfaces suggest a plausible model for the adhesive interaction.
 

Literature references that cite this PDB file's key reference

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Three-dimensional structure of cell adhesion molecules.
  Curr Opin Cell Biol, 8, 602-608.  
  8741846 H.de Nobel, P.N.Lipke, and J.Kurjan (1996).
Identification of a ligand-binding site in an immunoglobulin fold domain of the Saccharomyces cerevisiae adhesion protein alpha-agglutinin.
  Mol Biol Cell, 7, 143-153.  
8612071 J.M.McDonnell, A.J.Beavil, G.A.Mackay, B.A.Jameson, R.Korngold, H.J.Gould, and B.J.Sutton (1996).
Structure based design and characterization of peptides that inhibit IgE binding to its high-affinity receptor.
  Nat Struct Biol, 3, 419-426.  
8798624 L.B.Klickstein, M.R.York, A.R.Fougerolles, and T.A.Springer (1996).
Localization of the binding site on intercellular adhesion molecule-3 (ICAM-3) for lymphocyte function-associated antigen 1 (LFA-1).
  J Biol Chem, 271, 23920-23927.  
8636222 M.L.Dustin, L.M.Ferguson, P.Y.Chan, T.A.Springer, and D.E.Golan (1996).
Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area.
  J Cell Biol, 132, 465-474.  
8970726 M.Raghavan, and P.J.Bjorkman (1996).
Fc receptors and their interactions with immunoglobulins.
  Annu Rev Cell Dev Biol, 12, 181-220.  
8634239 M.S.McAlister, H.R.Mott, P.A.van der Merwe, I.D.Campbell, S.J.Davis, and P.C.Driscoll (1996).
NMR analysis of interacting soluble forms of the cell-cell recognition molecules CD2 and CD48.
  Biochemistry, 35, 5982-5991.  
8870072 P.Bork, A.K.Downing, B.Kieffer, and I.D.Campbell (1996).
Structure and distribution of modules in extracellular proteins.
  Q Rev Biophys, 29, 119-167.  
8913692 P.R.Crocker, and T.Feizi (1996).
Carbohydrate recognition systems: functional triads in cell-cell interactions.
  Curr Opin Struct Biol, 6, 679-691.  
8939697 S.E.O'Connor, and B.Imperiali (1996).
Modulation of protein structure and function by asparagine-linked glycosylation.
  Chem Biol, 3, 803-812.  
8805538 S.Improta, A.S.Politou, and A.Pastore (1996).
Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity.
  Structure, 4, 323-337.
PDB codes: 1tit 1tiu
8981082 S.Kelm, R.Schauer, and P.R.Crocker (1996).
The Sialoadhesins--a family of sialic acid-dependent cellular recognition molecules within the immunoglobulin superfamily.
  Glycoconj J, 13, 913-926.  
  8786236 W.A.Hendrickson (1996).
Production of crystallizable fragments of membrane proteins.
  J Bioenerg Biomembr, 28, 35-40.  
7638192 A.J.Murray, S.J.Lewis, A.N.Barclay, and R.L.Brady (1995).
One sequence, two folds: a metastable structure of CD2.
  Proc Natl Acad Sci U S A, 92, 7337-7341.
PDB code: 1cdc
7719344 A.O.Wilkie, S.F.Slaney, M.Oldridge, M.D.Poole, G.J.Ashworth, A.D.Hockley, R.D.Hayward, D.J.David, L.J.Pulleyn, and P.Rutland (1995).
Apert syndrome results from localized mutations of FGFR2 and is allelic with Crouzon syndrome.
  Nat Genet, 9, 165-172.  
8599667 A.S.Politou, D.J.Thomas, and A.Pastore (1995).
The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity.
  Biophys J, 69, 2601-2610.  
7822326 C.L.Holness, P.A.Bates, A.J.Little, C.D.Buckley, A.McDowall, D.Bossy, N.Hogg, and D.L.Simmons (1995).
Analysis of the binding site on intercellular adhesion molecule 3 for the leukocyte integrin lymphocyte function-associated antigen 1.
  J Biol Chem, 270, 877-884.  
7664116 C.M.Dobson (1995).
Finding the right fold.
  Nat Struct Biol, 2, 513-517.  
8749360 D.I.Stuart, and E.Y.Jones (1995).
Recognition at the cell surface: recent structural insights.
  Curr Opin Struct Biol, 5, 735-743.  
7539925 J.H.Wang, R.B.Pepinsky, T.Stehle, J.H.Liu, M.Karpusas, B.Browning, and L.Osborn (1995).
The crystal structure of an N-terminal two-domain fragment of vascular cell adhesion molecule 1 (VCAM-1): a cyclic peptide based on the domain 1 C-D loop can inhibit VCAM-1-alpha 4 integrin interaction.
  Proc Natl Acad Sci U S A, 92, 5714-5718.
PDB code: 1vsc
  7795530 L.A.Castonguay, S.H.Bryant, P.M.Snow, and J.S.Fetrow (1995).
A proposed structural model of domain 1 of fasciclin III neural cell adhesion protein based on an inverse folding algorithm.
  Protein Sci, 4, 472-483.  
7759486 L.Ge, A.Lupas, S.Peraldi-Roux, S.Spada, and A.Plückthun (1995).
A mouse Ig kappa domain of very unusual framework structure loses function when converted to the consensus.
  J Biol Chem, 270, 12446-12451.  
7528777 L.Osborn, E.S.Day, G.T.Miller, M.Karpusas, R.Tizard, S.C.Meuer, and P.S.Hochman (1995).
Amino acid residues required for binding of lymphocyte function-associated antigen 3 (CD58) to its counter-receptor CD2.
  J Exp Med, 181, 429-434.  
7624321 L.Shapiro, P.D.Kwong, A.M.Fannon, D.R.Colman, and W.A.Hendrickson (1995).
Considerations on the folding topology and evolutionary origin of cadherin domains.
  Proc Natl Acad Sci U S A, 92, 6793-6797.  
7892188 M.B.Keown, R.Ghirlando, R.J.Young, A.J.Beavil, R.J.Owens, S.J.Perkins, B.J.Sutton, and H.J.Gould (1995).
Hydrodynamic studies of a complex between the Fc fragment of human IgE and a soluble fragment of the Fc epsilon RI alpha chain.
  Proc Natl Acad Sci U S A, 92, 1841-1845.  
  8580836 M.J.Bennett, M.P.Schlunegger, and D.Eisenberg (1995).
3D domain swapping: a mechanism for oligomer assembly.
  Protein Sci, 4, 2455-2468.  
7697352 P.A.van der Merwe, P.N.McNamee, E.A.Davies, A.N.Barclay, and S.J.Davis (1995).
Topology of the CD2-CD48 cell-adhesion molecule complex: implications for antigen recognition by T cells.
  Curr Biol, 5, 74-84.  
7541042 P.S.Linsley, S.G.Nadler, J.Bajorath, R.Peach, H.T.Leung, J.Rogers, J.Bradshaw, M.Stebbins, G.Leytze, and W.Brady (1995).
Binding stoichiometry of the cytotoxic T lymphocyte-associated molecule-4 (CTLA-4). A disulfide-linked homodimer binds two CD86 molecules.
  J Biol Chem, 270, 15417-15424.  
7615513 R.W.Nelson, P.A.Bates, and U.Rutishauser (1995).
Protein determinants for specific polysialylation of the neural cell adhesion molecule.
  J Biol Chem, 270, 17171-17179.  
7529232 S.J.Davis, E.A.Davies, A.N.Barclay, S.Daenke, D.L.Bodian, E.Y.Jones, D.I.Stuart, T.D.Butters, R.A.Dwek, and P.A.van der Merwe (1995).
Ligand binding by the immunoglobulin superfamily recognition molecule CD2 is glycosylation-independent.
  J Biol Chem, 270, 369-375.  
7615642 U.Nörenberg, M.Hubert, T.Brümmendorf, A.Tárnok, and F.G.Rathjen (1995).
Characterization of functional domains of the tenascin-R (restrictin) polypeptide: cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by tenascin-R.
  J Cell Biol, 130, 473-484.  
  7668257 W.J.Park, C.Theda, N.E.Maestri, G.A.Meyers, J.S.Fryburg, C.Dufresne, M.M.Cohen, and E.W.Jabs (1995).
Analysis of phenotypic features and FGFR2 mutations in Apert syndrome.
  Am J Hum Genet, 57, 321-328.  
7606779 Z.Rao, P.Handford, M.Mayhew, V.Knott, G.G.Brownlee, and D.Stuart (1995).
The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions.
  Cell, 82, 131-141.
PDB code: 1edm
7512815 A.H.Huber, Y.M.Wang, A.J.Bieber, and P.J.Bjorkman (1994).
Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 A.
  Neuron, 12, 717-731.
PDB code: 1cfb
7525842 A.R.Arulanandam, A.Kister, M.J.McGregor, D.F.Wyss, G.Wagner, and E.L.Reinherz (1994).
Interaction between human CD2 and CD58 involves the major beta sheet surface of each of their respective adhesion domains.
  J Exp Med, 180, 1861-1871.  
7906650 A.S.Tavernor, J.H.Kydd, D.L.Bodian, E.Y.Jones, D.I.Stuart, S.J.Davis, and G.W.Butcher (1994).
Expression cloning of an equine T-lymphocyte glycoprotein CD2 cDNA. Structure-based analysis of conserved sequence elements.
  Eur J Biochem, 219, 969-976.  
8009170 B.Rubin, J.Arnaud, S.Caspar-Bauguil, F.Conte, and A.Huchenq (1994).
Biological function of the extracellular domain of the T-cell receptor constant region.
  Scand J Immunol, 39, 517-525.  
7994575 D.L.Bodian, E.Y.Jones, K.Harlos, D.I.Stuart, and S.J.Davis (1994).
Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
  Structure, 2, 755-766.
PDB code: 1hnf
7922025 G.Lange, S.J.Lewis, G.N.Murshudov, G.G.Dodson, P.C.Moody, J.P.Turkenburg, A.N.Barclay, and R.L.Brady (1994).
Crystal structure of an extracellular fragment of the rat CD4 receptor containing domains 3 and 4.
  Structure, 2, 469-481.  
7712288 G.Wagner, and D.F.Wyss (1994).
Cell surface adhesion receptors.
  Curr Opin Struct Biol, 4, 841-851.  
8020478 I.Callebaut, D.Portetelle, A.Burny, and J.P.Mornon (1994).
Identification of functional sites on bovine leukemia virus envelope glycoproteins using structural and immunological data.
  Eur J Biochem, 222, 405-414.  
8081748 I.D.Campbell, and C.Spitzfaden (1994).
Building proteins with fibronectin type III modules.
  Structure, 2, 333-337.  
7528140 T.J.Dudgeon, M.J.Bottomley, P.C.Driscoll, M.J.Humphries, A.P.Mould, G.I.Wingfield, and J.M.Clements (1994).
Expression and characterisation of a very-late antigen-4 (alpha 4 beta 1) integrin-binding fragment of vascular cell-adhesion molecule-1.
  Eur J Biochem, 226, 517-523.  
8103744 A.M.Carmo, D.W.Mason, and A.D.Beyers (1993).
Physical association of the cytoplasmic domain of CD2 with the tyrosine kinases p56lck and p59fyn.
  Eur J Immunol, 23, 2196-2201.  
7505442 A.R.Arulanandam, J.M.Withka, D.F.Wyss, G.Wagner, A.Kister, P.Pallai, M.A.Recny, and E.L.Reinherz (1993).
The CD58 (LFA-3) binding site is a localized and highly charged surface area on the AGFCC'C" face of the human CD2 adhesion domain.
  Proc Natl Acad Sci U S A, 90, 11613-11617.  
  8251933 A.W.Chan, E.G.Hutchinson, D.Harris, and J.M.Thornton (1993).
Identification, classification, and analysis of beta-bulges in proteins.
  Protein Sci, 2, 1574-1590.  
8347294 C.A.Janeway, and P.Golstein (1993).
Lymphocyte activation and effector functions. Editorial overview. The role of cell surface molecules.
  Curr Opin Immunol, 5, 313-323.  
7688025 C.Somoza, P.C.Driscoll, J.G.Cyster, and A.F.Williams (1993).
Mutational analysis of the CD2/CD58 interaction: the binding site for CD58 lies on one face of the first domain of human CD2.
  J Exp Med, 178, 549-558.  
8349740 H.Zhou, A.Fuks, G.Alcaraz, T.J.Bolling, and C.P.Stanners (1993).
Homophilic adhesion between Ig superfamily carcinoembryonic antigen molecules involves double reciprocal bonds.
  J Cell Biol, 122, 951-960.  
  7505680 J.Bajorath, R.Stenkamp, and A.Aruffo (1993).
Knowledge-based model building of proteins: concepts and examples.
  Protein Sci, 2, 1798-1810.
PDB code: 1kjd
8356059 J.F.Zagury, J.Bernard, A.Achour, A.Astgen, A.Lachgar, L.Fall, C.Carelli, W.Issing, J.P.Mbika, and O.Picard (1993).
Identification of CD4 and major histocompatibility complex functional peptide sites and their homology with oligopeptides from human immunodeficiency virus type 1 glycoprotein gp120: role in AIDS pathogenesis.
  Proc Natl Acad Sci U S A, 90, 7573-7577.  
  8102411 J.M.Rodríguez, R.J.Yáñez, F.Almazán, E.Viñuela, and J.F.Rodriguez (1993).
African swine fever virus encodes a CD2 homolog responsible for the adhesion of erythrocytes to infected cells.
  J Virol, 67, 5312-5320.  
7915183 J.M.Withka, D.F.Wyss, G.Wagner, A.R.Arulanandam, E.L.Reinherz, and M.A.Recny (1993).
Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2.
  Structure, 1, 69-81.
PDB code: 1cdb
8212315 M.A.Navia, and D.A.Peattie (1993).
Structure-based drug design: applications in immunopharmacology and immunosuppression.
  Trends Pharmacol Sci, 14, 189-195.  
8099016 P.A.van der Merwe, D.C.McPherson, M.H.Brown, A.N.Barclay, J.G.Cyster, A.F.Williams, and S.J.Davis (1993).
The NH2-terminal domain of rat CD2 binds rat CD48 with a low affinity and binding does not require glycosylation of CD2.
  Eur J Immunol, 23, 1373-1377.  
  7903240 P.A.van der Merwe, M.H.Brown, S.J.Davis, and A.N.Barclay (1993).
Affinity and kinetic analysis of the interaction of the cell adhesion molecules rat CD2 and CD48.
  EMBO J, 12, 4945-4954.  
8341653 P.Holliger, T.Prospero, and G.Winter (1993).
"Diabodies": small bivalent and bispecific antibody fragments.
  Proc Natl Acad Sci U S A, 90, 6444-6448.  
8260819 U.Rutishauser (1993).
Adhesion molecules of the nervous system.
  Curr Opin Neurobiol, 3, 709-715.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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