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1cid

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Revision as of 08:49, 24 December 2014

CRYSTAL STRUCTURE OF DOMAINS 3 & 4 OF RAT CD4 AND THEIR RELATIONSHIP TO THE NH2-TERMINAL DOMAINS

Structural highlights

1cid is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[CD4_RAT] Accessory protein for MHC class-II antigen/T-cell receptor interaction. May regulate T-cell activation.

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

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.

Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains.,Brady RL, Dodson EJ, Dodson GG, Lange G, Davis SJ, Williams AF, Barclay AN Science. 1993 May 14;260(5110):979-83. PMID:8493535^[1]

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

References

↑ Brady RL, Dodson EJ, Dodson GG, Lange G, Davis SJ, Williams AF, Barclay AN. Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains. Science. 1993 May 14;260(5110):979-83. PMID:8493535

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cid"

Categories: Rattus norvegicus | Brady, R L | Dodson, E J | Lange, G | T-cell surface glycoprotein

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cid OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cid RCSB], [http://www.ebi.ac.uk/pdbsum/1cid PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CD4_RAT CD4_RAT]] Accessory protein for MHC class-II antigen/T-cell receptor interaction. May regulate T-cell activation.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1cid

From Proteopedia

Revision as of 08:49, 24 December 2014

CRYSTAL STRUCTURE OF DOMAINS 3 & 4 OF RAT CD4 AND THEIR RELATIONSHIP TO THE NH2-TERMINAL DOMAINS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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