1hnf
From Proteopedia
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|PDB= 1hnf |SIZE=350|CAPTION= <scene name='initialview01'>1hnf</scene>, resolution 2.5Å | |PDB= 1hnf |SIZE=350|CAPTION= <scene name='initialview01'>1hnf</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hnf OCA], [http://www.ebi.ac.uk/pdbsum/1hnf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hnf RCSB]</span> | ||
}} | }} | ||
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[[Category: Jones, E Y.]] | [[Category: Jones, E Y.]] | ||
[[Category: Stuart, D I.]] | [[Category: Stuart, D I.]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: NAG]] | ||
[[Category: t lymphocyte adhesion glycoprotein]] | [[Category: t lymphocyte adhesion glycoprotein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:07:58 2008'' |
Revision as of 18:08, 30 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE EXTRACELLULAR REGION OF THE HUMAN CELL ADHESION MOLECULE CD2 AT 2.5 ANGSTROMS RESOLUTION
Overview
BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo. The extracellular regions of the human and rat homologues of CD2 share only 45% sequence identity and bind different protein ligands. Comparison of the human and rat soluble CD2 (sCD2) structures should provide insights into the structural basis of cell surface recognition. RESULTS: We therefore determined the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%. It is composed of two immunoglobulin superfamily domains similar to those of rat sCD2, but the relative orientation of the domains in the two homologues differs by up to 20 degrees. An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals. CONCLUSIONS: Intramolecular flexibility appears to be a conserved feature of CD2. The head-to-head interaction between molecules represents a general model for interactions between adhesion molecules of this structural class. Ligand specificity may be influenced by the distribution of charged residues on the binding face.
About this Structure
1HNF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution., Bodian DL, Jones EY, Harlos K, Stuart DI, Davis SJ, Structure. 1994 Aug 15;2(8):755-66. PMID:7994575
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