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Immune system
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PDB id
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2x44
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Contents |
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* Residue conservation analysis
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PDB id:
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Immune system
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Title:
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Structure of a strand-swapped dimeric form of ctla-4
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Structure:
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Cytotoxic t-lymphocyte protein 4. Chain: d. Fragment: residues 36-161. Synonym: cytotoxic t-lymphocyte-associated antigen 4, ctla- cd152, cytotoxic t-lymphocyte antigen 4. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Cell_line: jurkat. Tissue: blood. Cell: t-lymphocyte. Expressed in: escherichia coli. Expression_system_taxid: 469008. Other_details: cdna generated directly from jurkat cells, c
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Resolution:
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2.60Å
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R-factor:
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0.193
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R-free:
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0.245
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Authors:
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A.F.-P.Sonnen,C.Yu,E.J.Evans,D.I.Stuart,S.J.Davis, R.J.C.Gil
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Key ref:
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A.F.Sonnen
et al.
(2010).
Domain metastability: a molecular basis for immunoglobulin deposition?
J Mol Biol,
399,
207-213.
PubMed id:
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Date:
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28-Jan-10
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Release date:
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07-Apr-10
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PROCHECK
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Headers
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References
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P16410
(CTLA4_HUMAN) -
Cytotoxic T-lymphocyte protein 4
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Seq:
Struc:
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223 a.a.
121 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Gene Ontology (GO) functional annotation
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Cellular component
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membrane
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1 term
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Biological process
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immune response
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1 term
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J Mol Biol
399:207-213
(2010)
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PubMed id:
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Domain metastability: a molecular basis for immunoglobulin deposition?
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A.F.Sonnen,
C.Yu,
E.J.Evans,
D.I.Stuart,
S.J.Davis,
R.J.Gilbert.
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ABSTRACT
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We present the crystal structure of an immunoglobulin light-chain-like domain,
CTLA-4, as a strand-swapped dimer displaying cis-trans proline isomerisation and
native-like hydrogen bonding. We also show that CTLA-4 can form amyloid-like
fibres and amorphous deposits explainable by the same strand swapping. Our
results suggest a molecular basis for the pathological aggregation of
immunoglobulin domains and why amyloid-like fibres are more often composed of
homologous rather than heterologous subunits.
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Links
