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PDBsum entry 2hcc
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* Residue conservation analysis
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PDB id:
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Chemokine
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Title:
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Solution structure of the human chemokine hcc-2, nmr, 30 structures
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Structure:
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Human chemokine hcc-2. Chain: a. Fragment: residues 48-113 of hcc-2 precursor. Synonym: macrophage inflammatory protein 5 (mip-5), leukotactin-1. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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NMR struc:
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30 models
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Authors:
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H.Sticht,S.E.Escher,K.Schweimer,W.G.Forssmann,P.Roesch,K.Adermann
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Key ref:
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H.Sticht
et al.
(1999).
Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype.
Biochemistry,
38,
5995-6002.
PubMed id:
DOI:
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Date:
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03-Jul-98
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Release date:
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13-Jul-99
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PROCHECK
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Headers
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References
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Q16663
(CCL15_HUMAN) -
C-C motif chemokine 15 from Homo sapiens
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Seq:
Struc:
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113 a.a.
66 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Biochemistry
38:5995-6002
(1999)
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PubMed id:
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Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype.
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H.Sticht,
S.E.Escher,
K.Schweimer,
W.G.Forssmann,
P.Rösch,
K.Adermann.
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ABSTRACT
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HCC-2, a 66-amino acid residue human CC chemokine, was reported to induce
chemotaxis on monocytes, T-lymphocytes, and eosinophils. The three-dimensional
structure of HCC-2 has been determined by 1H nuclear magnetic resonance (NMR)
spectroscopy and restrained molecular dynamics calculations on the basis of 871
experimental restraints. The structure is well-defined, exhibiting average
root-mean-square deviations of 0.58 and 0.96 A for the backbone heavy atoms and
all heavy atoms of residues 5-63, respectively. In contrast to most other
chemokines, subtle structural differences impede dimer formation of HCC-2 in a
concentration range of 0.1 microM to 2 mM. HCC-2, however, exhibits the same
structural elements as the other chemokines, i.e., a triple-stranded
antiparallel beta-sheet covered by an alpha-helix, showing that the chemokine
fold is not influenced by quaternary interactions. Structural investigations
with a HCC-2 mutant prove that a third additional disulfide bond present in
wild-type HCC-2 is not necessary for maintaining the relative orientation of the
helix and the beta-sheet.
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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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R.R.Koenen,
P.von Hundelshausen,
I.V.Nesmelova,
A.Zernecke,
E.A.Liehn,
A.Sarabi,
B.K.Kramp,
A.M.Piccinini,
S.R.Paludan,
M.A.Kowalska,
A.J.Kungl,
T.M.Hackeng,
K.H.Mayo,
and
C.Weber
(2009).
Disrupting functional interactions between platelet chemokines inhibits atherosclerosis in hyperlipidemic mice.
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Nat Med,
15,
97.
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R.L.Tuinstra,
F.C.Peterson,
E.S.Elgin,
A.J.Pelzek,
and
B.F.Volkman
(2007).
An engineered second disulfide bond restricts lymphotactin/XCL1 to a chemokine-like conformation with XCR1 agonist activity.
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Biochemistry,
46,
2564-2573.
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PDB code:
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S.E.Escher,
U.Forssmann,
A.Frimpong-Boateng,
K.Adermann,
J.Vakili,
H.Sticht,
and
M.Detheux
(2004).
Functional analysis of chemically synthesized derivatives of the human CC chemokine CCL15/HCC-2, a high affinity CCR1 ligand.
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J Pept Res,
63,
36-47.
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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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E.S.Kuloğlu,
D.R.McCaslin,
J.L.Markley,
and
B.F.Volkman
(2002).
Structural rearrangement of human lymphotactin, a C chemokine, under physiological solution conditions.
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J Biol Chem,
277,
17863-17870.
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B.T.Seet,
R.Singh,
C.Paavola,
E.K.Lau,
T.M.Handel,
and
G.McFadden
(2001).
Molecular determinants for CC-chemokine recognition by a poxvirus CC-chemokine inhibitor.
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Proc Natl Acad Sci U S A,
98,
9008-9013.
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C.Baysal,
and
A.R.Atilgan
(2001).
Elucidating the structural mechanisms for biological activity of the chemokine family.
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Proteins,
43,
150-160.
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W.Shao,
E.Fernandez,
A.Sachpatzidis,
J.Wilken,
D.A.Thompson,
B.I.Schweitzer,
and
E.Lolis
(2001).
CCR2 and CCR5 receptor-binding properties of herpesvirus-8 vMIP-II based on sequence analysis and its solution structure.
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Eur J Biochem,
268,
2948-2959.
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PDB code:
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Buyong,
J.Xiong,
J.Lubkowski,
and
R.Nussinov
(2000).
Homology modeling and molecular dynamics simulations of lymphotactin.
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Protein Sci,
9,
2192-2199.
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J.S.Laurence,
C.Blanpain,
J.W.Burgner,
M.Parmentier,
and
P.J.LiWang
(2000).
CC chemokine MIP-1 beta can function as a monomer and depends on Phe13 for receptor binding.
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Biochemistry,
39,
3401-3409.
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J.T.Ashfield,
T.Meyers,
D.Lowne,
P.G.Varley,
J.R.Arnold,
P.Tan,
J.C.Yang,
L.G.Czaplewski,
T.Dudgeon,
and
J.Fisher
(2000).
Chemical modification of a variant of human MIP-1alpha; implications for dimer structure.
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Protein Sci,
9,
2047-2053.
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K.L.Mayer,
and
M.J.Stone
(2000).
NMR solution structure and receptor peptide binding of the CC chemokine eotaxin-2.
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Biochemistry,
39,
8382-8395.
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PDB codes:
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N.Gerber,
H.Lowman,
D.R.Artis,
and
C.Eigenbrot
(2000).
Receptor-binding conformation of the "ELR" motif of IL-8: X-ray structure of the L5C/H33C variant at 2.35 A resolution.
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Proteins,
38,
361-367.
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PDB code:
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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
