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PDBsum entry 5e6v
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Cell adhesion
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PDB id
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5e6v
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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 the crystal structure of the plexin-semaphorin- integrin domain/hybrid domain/i-egf1 segment from the human integrin b2 subunit
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Structure:
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Integrin beta-2. Chain: a. Fragment: unp residues 23-125, 365-482. Synonym: cell surface adhesion glycoproteins lfa-1/cr3/p150,95 subunit beta,complement receptor c3 subunit beta. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: itgb2, cd18, mfi7. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek. Expression_system_atcc_number: crl-3022
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Resolution:
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1.80Å
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R-factor:
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0.180
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R-free:
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0.229
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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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10-Oct-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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P05107
(ITB2_HUMAN) -
Integrin beta-2 from Homo sapiens
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Seq:
Struc:
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769 a.a.
224 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 4 residue positions (black
crosses)
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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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