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* Residue conservation analysis
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PDB id:
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Cell adhesion
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Title:
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Crystal structure of the extracellular segment of integrin alpha vbeta3 bound to mn2+
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Structure:
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Integrin alpha-v. Chain: a. Fragment: residues 31-987. Synonym: vitronectin receptor alpha subunit, cd51 antigen. Engineered: yes. Integrin beta-3. Chain: b. Fragment: residues 27-718. Synonym: platelet membrane glycoprotein iiia, gpiiia, cd61 antigen.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Cell_line: sf9. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
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Biol. unit:
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Tetramer (from
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Resolution:
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3.30Å
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R-factor:
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0.244
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R-free:
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0.323
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Authors:
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J.-P.Xiong,T.Stehle,R.Zhang,A.Joachimiak,M.Frech,S.L.Goodman, M.A.Arnaout
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Key ref:
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J.P.Xiong
et al.
(2002).
Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand.
Science,
296,
151-155.
PubMed id:
DOI:
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Date:
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20-Jun-02
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Release date:
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14-Aug-02
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PROCHECK
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Headers
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References
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DOI no:
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Science
296:151-155
(2002)
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PubMed id:
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Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand.
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J.P.Xiong,
T.Stehle,
R.Zhang,
A.Joachimiak,
M.Frech,
S.L.Goodman,
M.A.Arnaout.
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ABSTRACT
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The structural basis for the divalent cation-dependent binding of heterodimeric
alphabeta integrins to their ligands, which contain the prototypical Arg-Gly-Asp
sequence, is unknown. Interaction with ligands triggers tertiary and quaternary
structural rearrangements in integrins that are needed for cell signaling. Here
we report the crystal structure of the extracellular segment of integrin
alphaVbeta3 in complex with a cyclic peptide presenting the Arg-Gly-Asp
sequence. The ligand binds at the major interface between the alphaV and beta3
subunits and makes extensive contacts with both. Both tertiary and quaternary
changes are observed in the presence of ligand. The tertiary rearrangements take
place in betaA, the ligand-binding domain of beta3; in the complex, betaA
acquires two cations, one of which contacts the ligand Asp directly and the
other stabilizes the ligand-binding surface. Ligand binding induces small
changes in the orientation of alphaV relative to beta3.
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Selected figure(s)
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Figure 2.
Fig. 2. The ligand-integrin binding site. (A) Surface
representation of the ligand-binding site, with the ligand
peptide shown as ball-and-stick model. Color code for the ligand
and the two visible Mn2+ ions (MIDAS and ADMIDAS) is as in Fig.
1. (B) Interactions between ligand and integrin. The peptide
(yellow) and residues interacting with the ligand or with Mn2+
ions are shown in ball-and-stick representation.  V and  3 residues
are labeled blue and red, respectively. Oxygen and nitrogen
atoms are in red and blue, respectively. The three Mn2+ ions in
3 at MIDAS,
ADMIDAS, and LIMBS are also shown. Hydrogen bonds and salt
bridges (distance cutoff, 3.5 Å) are represented with
dotted lines.
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Figure 3.
Fig. 3. Diagram of the MIDAS motif in A (A and B)
and A from
CD11b (C and D). (A) and (B) MIDAS residues (single letter
abbreviations: S, Ser; E, Glu; D, Asp; T, Thr) in unliganded (A)
and liganded (B) A.
Coordinating side chains are shown in ball-and-stick
representations with oxygen atoms in red, carbon in green; the
ligand aspartate is in gold. In addition to the ligand
aspartate, the Mn2+ (cyan) in the A MIDAS is
coordinated directly with the hydroxyl oxygens of Ser121 and
Ser123 and with one carboxylate oxygen from Glu220. The carboxyl
oxygens of Asp119 and Asp251 of A lie
within 6Å of the metal ion and likely mediate additional
contacts through water molecules similar to the liganded forms
of A (D). The
Mn2+ ion at ADMIDAS (magenta) is present in (A) and (B). The
Mn2+ ions at MIDAS and at LIMBS (cyan and gray, respectively)
are only present in (B). (C) and (D) MIDAS residues in
unliganded (C) and liganded (D) A from
CD11b. The metal ion (cyan) is present in both. Water molecules
are labeled  ; the
pseudoligand glutamate is in gold. Hydrogen bonds and metal ion
coordination are represented with dotted yellow lines.
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The above figures are
reprinted
by permission from the AAAs:
Science
(2002,
296,
151-155)
copyright 2002.
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Figures were
selected
by an automated process.
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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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Nature,
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PDB codes:
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W.Sebald,
J.Nickel,
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PDB code:
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PDB code:
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Mass spectrometric based mapping of the disulfide bonding patterns of integrin alpha chains.
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Biochemistry,
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R.Alon,
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LAD-III, a novel group of leukocyte integrin activation deficiencies.
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Trends Immunol,
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A tumor-associated beta 1 integrin mutation that abrogates epithelial differentiation control.
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J Cell Biol,
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Integrin beta3 Leu33Pro homozygosity and risk of cancer.
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J Natl Cancer Inst,
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Three-dimensional model of the human platelet integrin alpha IIbbeta 3 based on electron cryomicroscopy and x-ray crystallography.
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Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein.
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J Cell Biol,
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R.L.Wilder
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Integrin alpha V beta 3 as a target for treatment of rheumatoid arthritis and related rheumatic diseases.
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Concerted action of androgens and mechanical strain shifts bone metabolism from high turnover into an osteoanabolic mode.
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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
codes are
shown on the right.
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 |
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