Structure analysis

Structural basis for the recognition of mutant self by a tumor-specific, MHC class II-restricted T cell receptor G4

X-ray diffraction
2.6Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero pentamer (preferred)
Entry contents: 5 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero pentamer
Accessible surface area: 35600 Å2
Buried surface area: 13800 Å2
Dissociation area: 1,200 Å2
Dissociation energy (ΔGdiss): -3 kcal/mol
Dissociation entropy (TΔSdiss): 14 kcal/mol
Interface energy (ΔGint): -77 kcal/mol
Symmetry number: 1
Assembly 2
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Multimeric state: hetero pentamer
Accessible surface area: 35300 Å2
Buried surface area: 13700 Å2
Dissociation area: 1,200 Å2
Dissociation energy (ΔGdiss): -4 kcal/mol
Dissociation entropy (TΔSdiss): 14 kcal/mol
Interface energy (ΔGint): -65 kcal/mol
Symmetry number: 1

Macromolecules

Chains: C, H
Length: 15 amino acids
Theoretical weight: 1.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P60174 (Residues: 60-74; Coverage: 5%)
Gene names: TPI, TPI1

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Chains: E, J
Length: 239 amino acids
Theoretical weight: 27.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
InterPro:
CATH: Immunoglobulins

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Chains: D, I
Length: 203 amino acids
Theoretical weight: 22.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
InterPro:
CATH: Immunoglobulins

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