 |
PDBsum entry 1cid
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
T-cell surface glycoprotein
|
PDB id
|
|
|
|
1cid
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of domains 3 and 4 of rat cd4: relation to the nh2-Terminal domains.
|
|
|
Authors
|
|
R.L.Brady,
E.J.Dodson,
G.G.Dodson,
G.Lange,
S.J.Davis,
A.F.Williams,
A.N.Barclay.
|
|
|
Ref.
|
|
Science, 1993,
260,
979-983.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
84%.
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|
|
|
|
