1cid: Difference between revisions
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[[Image:1cid.gif|left|200px]] | [[Image:1cid.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF DOMAINS 3 & 4 OF RAT CD4 AND THEIR RELATIONSHIP TO THE NH2-TERMINAL DOMAINS''' | {{Structure | ||
|PDB= 1cid |SIZE=350|CAPTION= <scene name='initialview01'>1cid</scene>, resolution 2.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF DOMAINS 3 & 4 OF RAT CD4 AND THEIR RELATIONSHIP TO THE NH2-TERMINAL DOMAINS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CID is a [ | 1CID is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CID OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8493535 8493535] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: t-cell surface glycoprotein]] | [[Category: t-cell surface glycoprotein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:24:45 2008'' | ||
Revision as of 11:24, 20 March 2008
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CRYSTAL STRUCTURE OF DOMAINS 3 & 4 OF RAT CD4 AND THEIR RELATIONSHIP TO THE NH2-TERMINAL DOMAINS
OverviewOverview
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.
About this StructureAbout this Structure
1CID is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
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
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