1cd8: Difference between revisions

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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cd8 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cd8 ConSurf].
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== Publication Abstract from PubMed ==
A secreted fragment of the extracellular portion of human CD8 alpha has been expressed in CHO cells, and a deglycosylated and proteolyzed form of this fragment has been crystallized. We report here the crystal structure of this fragment as refined at 2.6 A resolution. The structure was solved by molecular replacement using a superposition of ten variable domains from immunoglobulin light chains as the search model. Only the N-terminal 114 amino acids of CD8 alpha are visible in the electron density maps. The domain formed by these residues possesses a fold typical of immunoglobulin variable domains and associates to form Fv-like homodimers.
Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 A resolution.,Leahy DJ, Axel R, Hendrickson WA Cell. 1992 Mar 20;68(6):1145-62. PMID:1547508<ref>PMID:1547508</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
==See Also==
*[[CD8 3D structures|CD8 3D structures]]
*[[CD8 3D structures|CD8 3D structures]]
== References ==
<references/>
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__TOC__
</StructureSection>
</StructureSection>

Revision as of 08:26, 5 June 2024

CRYSTAL STRUCTURE OF A SOLUBLE FORM OF THE HUMAN T CELL CO-RECEPTOR CD8 AT 2.6 ANGSTROMS RESOLUTIONCRYSTAL STRUCTURE OF A SOLUBLE FORM OF THE HUMAN T CELL CO-RECEPTOR CD8 AT 2.6 ANGSTROMS RESOLUTION

Structural highlights

1cd8 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

CD8A_HUMAN Defects in CD8A are a cause of familial CD8 deficiency (CD8 deficiency) [MIM:608957. Familial CD8 deficiency is a novel autosomal recessive immunologic defect characterized by absence of CD8+ cells, leading to recurrent bacterial infections.

Function

CD8A_HUMAN Identifies cytotoxic/suppressor T-cells that interact with MHC class I bearing targets. CD8 is thought to play a role in the process of T-cell mediated killing. CD8 alpha chains binds to class I MHC molecules alpha-3 domains.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

A secreted fragment of the extracellular portion of human CD8 alpha has been expressed in CHO cells, and a deglycosylated and proteolyzed form of this fragment has been crystallized. We report here the crystal structure of this fragment as refined at 2.6 A resolution. The structure was solved by molecular replacement using a superposition of ten variable domains from immunoglobulin light chains as the search model. Only the N-terminal 114 amino acids of CD8 alpha are visible in the electron density maps. The domain formed by these residues possesses a fold typical of immunoglobulin variable domains and associates to form Fv-like homodimers.

Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 A resolution.,Leahy DJ, Axel R, Hendrickson WA Cell. 1992 Mar 20;68(6):1145-62. PMID:1547508[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Leahy DJ, Axel R, Hendrickson WA. Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 A resolution. Cell. 1992 Mar 20;68(6):1145-62. PMID:1547508

1cd8, resolution 2.60Å

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OCA