1cid: Difference between revisions

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{{STRUCTURE_1cid|  PDB=1cid  |  SCENE=  }}  
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'''CRYSTAL STRUCTURE OF DOMAINS 3 & 4 OF RAT CD4 AND THEIR RELATIONSHIP TO THE NH2-TERMINAL DOMAINS'''
===CRYSTAL STRUCTURE OF DOMAINS 3 & 4 OF RAT CD4 AND THEIR RELATIONSHIP TO THE NH2-TERMINAL DOMAINS===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Lange, G.]]
[[Category: Lange, G.]]
[[Category: T-cell surface glycoprotein]]
[[Category: T-cell surface glycoprotein]]
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Revision as of 20:47, 30 June 2008

File:1cid.png

Template:STRUCTURE 1cid

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

Template:ABSTRACT PUBMED 8493535

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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