1CDB

STRUCTURE OF THE GLYCOSYLATED ADHESION DOMAIN OF HUMAN T LYMPHOCYTE GLYCOPROTEIN CD2


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Submitted: 18 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2.

Withka, J.M.Wyss, D.F.Wagner, G.Arulanandam, A.R.Reinherz, E.L.Recny, M.A.

(1993) Structure 1: 69-81

  • DOI: https://doi.org/10.1016/0969-2126(93)90009-6
  • Primary Citation of Related Structures:  
    1CDB

  • PubMed Abstract: 

    CD2, a T-cell specific surface glycoprotein, is critically important for mediating adherence of T cells to antigen-presenting cells or target cells. Domain 1 of human CD2 is responsible for cell adhesion, binding to CD58 (LFA-3) expressed on the cell to which the T cell binds. Human CD2 domain 1 requires N-linked carbohydrate to maintain its native conformation and ability to bind CD58. In contrast, rat CD2 does not require N-linked carbohydrate, and binds to a different ligand, CD48.


  • Organizational Affiliation

    Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CD2105Homo sapiensMutation(s): 0 
Gene Names: POTENTIAL
UniProt & NIH Common Fund Data Resources
Find proteins for P06729 (Homo sapiens)
Explore P06729 
Go to UniProtKB:  P06729
PHAROS:  P06729
GTEx:  ENSG00000116824 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP06729
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Submitted: 18 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1994-01-31
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-16
    Changes: Database references, Derived calculations, Other