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PDBsum entry 3k72
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Cell adhesion
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PDB id
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3k72
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Contents |
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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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Structure of integrin alphax beta2
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Structure:
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Integrin alpha-x. Chain: a, c. Fragment: residues 20-1103. Synonym: leukocyte adhesion glycoprotein p150,95 alpha chain, leukocyte adhesion receptor p150,95, leu m5, cd11 antigen-like family member c. Engineered: yes. Integrin beta-2. Chain: b, d.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: cd11c, itgax. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Gene: cd18, itgb2, mfi7.
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Resolution:
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3.70Å
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R-factor:
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0.315
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R-free:
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0.335
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Authors:
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C.Xie,J.Zhu,X.Chen,L.Mi,N.Nishida,T.A.Springer
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Key ref:
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C.Xie
et al.
(2010).
Structure of an integrin with an alphaI domain, complement receptor type 4.
Embo J,
29,
666-679.
PubMed id:
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Date:
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11-Oct-09
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Release date:
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12-Jan-10
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PROCHECK
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Headers
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References
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Embo J
29:666-679
(2010)
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PubMed id:
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Structure of an integrin with an alphaI domain, complement receptor type 4.
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C.Xie,
J.Zhu,
X.Chen,
L.Mi,
N.Nishida,
T.A.Springer.
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ABSTRACT
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We report the structure of an integrin with an alphaI domain, alpha(X)beta(2),
the complement receptor type 4. It was earlier expected that a fixed orientation
between the alphaI domain and the beta-propeller domain in which it is inserted
would be required for allosteric signal transmission. However, the alphaI domain
is highly flexible, enabling two betaI domain conformational states to couple to
three alphaI domain states, and greater accessibility for ligand recognition.
Although alpha(X)beta(2) is bent similarly to integrins that lack alphaI
domains, the terminal domains of the alpha- and beta-legs, calf-2 and beta-tail,
are oriented differently than in alphaI-less integrins. Linkers extending to the
transmembrane domains are unstructured. Previous mutations in the beta(2)-tail
domain support the importance of extension, rather than a deadbolt, in integrin
activation. The locations of further activating mutations and antibody epitopes
show the critical role of extension, and conversion from the closed to the open
headpiece conformation, in integrin activation. Differences among 10 molecules
in crystal lattices provide unprecedented information on interdomain flexibility
important for modelling integrin extension and activation.
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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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N.J.Anthis,
and
I.D.Campbell
(2011).
The tail of integrin activation.
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Trends Biochem Sci,
36,
191-198.
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W.Chen,
J.Lou,
J.Hsin,
K.Schulten,
S.C.Harvey,
and
C.Zhu
(2011).
Molecular dynamics simulations of forced unbending of integrin α(v)β₃.
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PLoS Comput Biol,
7,
e1001086.
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C.Rosano,
and
M.Rocco
(2010).
Solution properties of full-length integrin alpha(IIb)beta3 refined models suggest environment-dependent induction of alternative bent /extended resting states.
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FEBS J,
277,
3190-3202.
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D.Cox,
M.Brennan,
and
N.Moran
(2010).
Integrins as therapeutic targets: lessons and opportunities.
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Nat Rev Drug Discov,
9,
804-820.
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J.Zhu,
J.Zhu,
A.Negri,
D.Provasi,
M.Filizola,
B.S.Coller,
and
T.A.Springer
(2010).
Closed headpiece of integrin αIIbβ3 and its complex with an αIIbβ3-specific antagonist that does not induce opening.
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Blood,
116,
5050-5059.
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PDB codes:
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M.E.Call,
and
J.J.Chou
(2010).
A view into the blind spot: solution NMR provides new insights into signal transduction across the lipid bilayer.
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Structure,
18,
1559-1569.
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N.J.Anthis,
K.L.Wegener,
D.R.Critchley,
and
I.D.Campbell
(2010).
Structural diversity in integrin/talin interactions.
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Structure,
18,
1654-1666.
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X.Chen,
C.Xie,
N.Nishida,
Z.Li,
T.Walz,
and
T.A.Springer
(2010).
Requirement of open headpiece conformation for activation of leukocyte integrin alphaXbeta2.
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Proc Natl Acad Sci U S A,
107,
14727-14732.
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Y.Pan,
K.Zhang,
J.Qi,
J.Yue,
T.A.Springer,
and
J.Chen
(2010).
Cation-pi interaction regulates ligand-binding affinity and signaling of integrin alpha4beta7.
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Proc Natl Acad Sci U S A,
107,
21388-21393.
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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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Links
