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Immune system
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PDB id
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1el0
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Contents |
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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extracellular region
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1 term
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Biological process
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immune response
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1 term
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Biochemical function
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chemokine activity
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1 term
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DOI no:
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Biochemistry
39:6053-6059
(2000)
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PubMed id:
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Human CC chemokine I-309, structural consequences of the additional disulfide bond.
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D.W.Keizer,
M.P.Crump,
T.W.Lee,
C.M.Slupsky,
I.Clark-Lewis,
B.D.Sykes.
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ABSTRACT
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I-309 is a member of the CC subclass of chemokines and is one of only three
human chemokines known to contain an additional, third disulfide bond. The
three-dimensional solution structure of I-309 was determined by (1)H nuclear
magnetic resonance spectroscopy and dynamic simulated annealing. The structure
of I-309, which remains monomeric at high concentrations, was determined on the
basis of 978 experimental restraints. The N-terminal region of I-309 was
disordered, as has been previously observed for the CC chemokine eotaxin but not
others such as MCP-1 and RANTES. This was followed in I-309 by a well-ordered
region between residues 13 and 69 that consisted of a 3(10)-helix, a
triple-stranded antiparallel beta-sheet, and finally a C-terminal alpha-helix.
Root-mean-square deviations of 0.61 and 1.16 were observed for the backbone and
heavy atoms, respectively. A comparison of I-309 to eotaxin and HCC-2 revealed a
significant structural change in the C-terminal region of the protein. The
alpha-helix normally present in chemokines was terminated early and was followed
by a short section of extended strand. These changes were a direct result of the
additional disulfide bond present in this protein. An examination of the I-309
structure will aid in an understanding of the specificity of this protein with
its receptor, CCR8.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.I.Chan,
H.N.Hunter,
B.F.Tack,
and
H.J.Vogel
(2008).
Human macrophage inflammatory protein 3alpha: protein and peptide nuclear magnetic resonance solution structures, dimerization, dynamics, and anti-infective properties.
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Antimicrob Agents Chemother, 52,
883-894.
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PDB code:
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A.E.Proudfoot,
T.M.Handel,
Z.Johnson,
E.K.Lau,
P.LiWang,
I.Clark-Lewis,
F.Borlat,
T.N.Wells,
and
M.H.Kosco-Vilbois
(2003).
Glycosaminoglycan binding and oligomerization are essential for the in vivo activity of certain chemokines.
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Proc Natl Acad Sci U S A, 100,
1885-1890.
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O.A.Asojo,
C.Boulègue,
D.M.Hoover,
W.Lu,
and
J.Lubkowski
(2003).
Structures of thymus and activation-regulated chemokine (TARC).
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Acta Crystallogr D Biol Crystallogr, 59,
1165-1173.
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PDB codes:
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E.J.Fernandez,
and
E.Lolis
(2002).
Structure, function, and inhibition of chemokines.
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Annu Rev Pharmacol Toxicol, 42,
469-499.
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T.S.Stantchev,
and
C.C.Broder
(2001).
Human immunodeficiency virus type-1 and chemokines: beyond competition for common cellular receptors.
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Cytokine Growth Factor Rev, 12,
219-243.
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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.
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Links
