 |
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
|
|
|
|
|
|
Gene Ontology (GO) functional annotation
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Cellular component
|
extracellular region
|
2 terms
|
|
|
Biological process
|
immune response
|
2 terms
|
|
|
Biochemical function
|
growth factor activity
|
2 terms
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
J Struct Biol
107:189-195
(1991)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
The structure of murine interleukin-1 beta at 2.8 A resolution.
|
|
J.van Oostrum,
J.P.Priestle,
M.G.Grütter,
A.Schmitz.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
The three-dimensional structure of recombinant murine interleukin-1 beta has
been solved by X-ray crystallographic techniques to 2.8 A resolution and refined
to a crystallographic R factor of 0.192. Although murine interleukin-1 beta
crystallizes in the same space group as human interleukin-1 beta with almost
identical unit cell dimensions, the packing of the molecules is quite different.
The murine interleukin-1 beta structure was solved by molecular replacement
using the refined structure of human interleukin-1 beta as trial structure, and
found to be related to the human structure by a nearly perfect twofold rotation
about the crystallographic y-axis and a 14 degrees rotation about the z-axis,
with no translation. The folding of murine interleukin-1 beta is similar to that
found for the human variant, consisting of 12 beta strands wrapped around a core
of hydrophobic side chains in a tetrahedron-like fashion. Significant
differences with respect to the human structure are seen at the N terminus and
in 4 of the 11 loops connecting the 12 beta strands.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
M.G.Rudolph,
M.S.Kelker,
T.R.Schneider,
T.O.Yeates,
V.Oseroff,
D.K.Heidary,
P.A.Jennings,
and
I.A.Wilson
(2003).
Use of multiple anomalous dispersion to phase highly merohedrally twinned crystals of interleukin-1beta.
|
| |
Acta Crystallogr D Biol Crystallogr, 59,
290-298.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
J.M.Thornton
(2001).
The Hans Neurath Award lecture of The Protein Society: proteins-- a testament to physics, chemistry, and evolution.
|
| |
Protein Sci, 10,
3.
|
|
|
|
|
|
|
N.E.Robinson,
and
A.B.Robinson
(2001).
Prediction of protein deamidation rates from primary and three-dimensional structure.
|
| |
Proc Natl Acad Sci U S A, 98,
4367-4372.
|
|
|
|
|
|
|
H.A.Schreuder,
J.M.Rondeau,
C.Tardif,
A.Soffientini,
E.Sarubbi,
A.Akeson,
T.L.Bowlin,
S.Yanofsky,
and
R.W.Barrett
(1995).
Refined crystal structure of the interleukin-1 receptor antagonist. Presence of a disulfide link and a cis-proline.
|
| |
Eur J Biochem, 227,
838-847.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
K.Schotanus,
R.H.Meloen,
W.C.Puijk,
F.Berkenbosch,
R.Binnekade,
and
F.J.Tilders
(1995).
Effects of monoclonal antibodies to specific epitopes of rat interleukin-1 beta (IL-1 beta) on IL-1 beta-induced ACTH, corticosterone and IL-6 responses in rats.
|
| |
J Neuroendocrinol, 7,
255-262.
|
|
|
|
|
|
|
P.R.Young
(1992).
Protein hormones and their receptors.
|
| |
Curr Opin Biotechnol, 3,
408-421.
|
|
|
|
|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
|
|
Links
