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PDBsum entry 5es4
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Cell adhesion
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PDB id
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5es4
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Contents |
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1080 a.a.
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674 a.a.
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884 a.a.
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PDB id:
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| Name: |
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Cell adhesion
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Title:
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Re-refinement of integrin alphaxbeta2 ectodomain in the closed/bent conformation
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Structure:
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Integrin alpha-x. Chain: a, c, e, g. Fragment: unp residues 20-1103. Synonym: cd11 antigen-like family member c,leu m5,leukocyte adhesion glycoprotein p150,95 alpha chain,leukocyte adhesion receptor p150,95. Engineered: yes. Integrin beta-2. Chain: b, d, f, h. Fragment: unp residues 23-696.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: itgax, cd11c. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Gene: itgb2, cd18, mfi7. Expression_system_taxid: 10029
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Resolution:
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3.30Å
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R-factor:
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0.258
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R-free:
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0.307
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Authors:
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M.Sen,T.A.Springer
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Key ref:
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M.Sen
and
T.A.Springer
(2016).
Leukocyte integrin αLβ2 headpiece structures: The αI domain, the pocket for the internal ligand, and concerted movements of its loops.
Proc Natl Acad Sci U S A,
113,
2940-2945.
PubMed id:
DOI:
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Date:
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16-Nov-15
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Release date:
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02-Mar-16
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PROCHECK
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Headers
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References
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P20702
(ITAX_HUMAN) -
Integrin alpha-X from Homo sapiens
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Seq:
Struc:
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1163 a.a.
1080 a.a.
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DOI no:
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Proc Natl Acad Sci U S A
113:2940-2945
(2016)
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PubMed id:
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Leukocyte integrin αLβ2 headpiece structures: The αI domain, the pocket for the internal ligand, and concerted movements of its loops.
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M.Sen,
T.A.Springer.
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ABSTRACT
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High-resolution crystal structures of the headpiece of lymphocyte
function-associated antigen-1 (integrin αLβ2) reveal how the αI domain
interacts with its platform formed by the α-subunit β-propeller and β-subunit
βI domains. The αLβ2 structures compared with αXβ2 structures show that the
αI domain, tethered through its N-linker and a disulfide to a stable β-ribbon
pillar near the center of the platform, can undergo remarkable pivoting and
tilting motions that appear buffered by N-glycan decorations that differ between
αL and αX subunits. Rerefined β2 integrin structures reveal details including
pyroglutamic acid at the β2 N terminus and bending within the EGF1 domain.
Allostery is relayed to the αI domain by an internal ligand that binds to a
pocket at the interface between the β-propeller and βI domains. Marked
differences between the αL and αX subunit β-propeller domains concentrate
near the binding pocket and αI domain interfaces. Remarkably, movement in
allostery in the βI domain of specificity determining loop 1 (SDL1) causes
concerted movement of SDL2 and thereby tightens the binding pocket for the
internal ligand.
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