Structure analysis

Structural basis for recognition of mutant self by a tumor-specific, MHC class II-restricted TCR

X-ray diffraction
2.8Å 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: 36028.47 Å2
Buried surface area: 13960.4 Å2
Dissociation area: 1,276.78 Å2
Dissociation energy (ΔGdiss): 0.51 kcal/mol
Dissociation entropy (TΔSdiss): 13.89 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-134726

Macromolecules

Chain: P
Length: 15 amino acids
Theoretical weight: 1.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P60174 (Residues: 23-37; Coverage: 6%)
Gene names: TPI, TPI1

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Chain: C
Length: 202 amino acids
Theoretical weight: 22.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P01848 (Residues: 1-93; Coverage: 66%)
Gene names: TCRA, TRAC
Pfam: Domain of unknown function (DUF1968)
InterPro:
CATH: Immunoglobulins

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Chain: D
Length: 240 amino acids
Theoretical weight: 27.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P01850 (Residues: 1-129; Coverage: 73%)
Gene name: TRBC1
Pfam: Immunoglobulin C1-set domain
InterPro:
CATH: Immunoglobulins

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