Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon' - sprookjes - yvandenbroek - TriplyDB

Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'

Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'

http://www.wikidata.org/entity/Q27647150

about

Large scale characterization of the LC13 TCR and HLA-B8 structural landscape in reaction to 172 altered peptide ligands: a molecular dynamics simulation study Coevolution of T-cell receptors with MHC and non-MHC ligands Structural basis of metal hypersensitivity Epitope flexibility and dynamic footprint revealed by molecular dynamics of a pMHC-TCR complex Differential Recognition of CD1d-α-Galactosyl Ceramide by the Vβ8.2 and Vβ7 Semi-invariant NKT T Cell Receptors Crossreactive T Cells Spotlight the Germline Rules for αβ T Cell-Receptor Interactions with MHC Molecules How a T Cell Receptor-like Antibody Recognizes Major Histocompatibility Complex-bound Peptide Distinct CDR3 conformations in TCRs determine the level of cross-reactivity for diverse antigens, but not the docking orientation Natural micropolymorphism in human leukocyte antigens provides a basis for genetic control of antigen recognition Germ Line-governed Recognition of a Cancer Epitope by an Immunodominant Human T-cell Receptor Hard wiring of T cell receptor specificity for the major histocompatibility complex is underpinned by TCR adaptability Allelic polymorphism in the T cell receptor and its impact on immune responses A highly tilted binding mode by a self-reactive T cell receptor results in altered engagement of peptide and MHC Conformational Melding Permits a Conserved Binding Geometry in TCR Recognition of Foreign and Self Molecular Mimics Structure of a TCR with high affinity for self-antigen reveals basis for escape from negative selection Structural Basis of Specificity and Cross-Reactivity in T Cell Receptors Specific for Cytochrome c-I-E Structural basis for enabling T-cell receptor diversity within biased virus-specific CD8+ T-cell responses A semi-invariant Vα10+ T cell antigen receptor defines a population of natural killer T cells with distinct glycolipid antigen-recognition properties A Single T Cell Receptor Bound to Major Histocompatibility Complex Class I and Class II Glycoproteins Reveals Switchable TCR Conformers TCRs Used in Cancer Gene Therapy Cross-React with MART-1/Melan-A Tumor Antigens via Distinct Mechanisms T-cell receptor (TCR) interaction with peptides that mimic nickel offers insight into nickel contact allergy V 2 natural killer T cell antigen receptor-mediated recognition of CD1d-glycolipid antigen T Cell Receptor Signaling Is Limited by Docking Geometry to Peptide-Major Histocompatibility Complex Structural basis for the killing of human beta cells by CD8(+) T cells in type 1 diabetes.Highly Divergent T-cell Receptor Binding Modes Underlie Specific Recognition of a Bulged Viral Peptide bound to a Human Leukocyte Antigen Class I Molecule The Energetic Basis Underpinning T-cell Receptor Recognition of a Super-bulged Peptide Bound to a Major Histocompatibility Complex Class I Molecule Lysophospholipid presentation by CD1d and recognition by a human Natural Killer T-cell receptor Crystal structure of a complete ternary complex of T-cell receptor, peptide-MHC, and CD4 A Conserved Hydrophobic Patch on Vβ Domains Revealed by TCRβ Chain Crystal Structures: Implications for Pre-TCR Dimerization Crossreactivity of a human autoimmune TCR is dominated by a single TCR loop T-cell Receptor (TCR)-Peptide Specificity Overrides Affinity-enhancing TCR-Major Histocompatibility Complex Interactions Effect of CDR3 Sequences and Distal V Gene Residues in Regulating TCR-MHC Contacts and Ligand Specificity T cell receptor reversed polarity recognition of a self-antigen major histocompatibility complex Germline-encoded amino acids in the alphabeta T-cell receptor control thymic selection αβ T cell receptors that do not undergo major histocompatibility complex-specific thymic selection possess antibody-like recognition specificities MHC restriction is imposed on a diverse T cell receptor repertoire by CD4 and CD8 co-receptors during thymic selection Reconciling views on T cell receptor germline bias for MHC Structural insights into the editing of germ-line-encoded interactions between T-cell receptor and MHC class II by Vα CDR3 T cells and their eons-old obsession with MHC Lck availability during thymic selection determines the recognition specificity of the T cell repertoire

P2860

Q24288783-28C0BD01-FDB8-4AE0-87E3-7D73E275AFC3 Q26797242-965CA48B-75D7-4984-8DAE-497BE0338761 Q26853141-228B00EE-BE4E-4830-9933-D2BD340CE325 Q27331858-AFFDB1B3-EC6B-4AE9-AFE1-95D93862E717 Q27646525-220753C4-9490-4CCC-8F44-E04F3713E828 Q27649963-064E0CD6-C64E-42DA-8B8B-9BADAC7855B4 Q27651585-ADCE0FD5-F9A5-4BEA-BDBC-525098D952C2 Q27652612-B706E345-D6FC-4AD3-85C2-E960FA88A6A8 Q27653404-1AC609FB-AD3E-42F1-B328-1AE5EF9318F0 Q27656470-D2A58488-F8F6-4556-8001-8A7DA43DFB43 Q27661747-9768F249-22E3-47F6-91CC-FD33EA177B34 Q27662550-F3FCDB29-3D21-41EA-B952-5B0BBFEA699F Q27666431-6533DB41-BC57-4E9B-9747-3519232AC5FA Q27666797-0FDE4928-D84A-4CF1-A928-F9A8602E0F40 Q27666863-2731248B-FF1A-44D1-BE86-61FBF1A84006 Q27667507-FB087328-FCF2-4B2D-9E8A-09063BEB2068 Q27667972-617AA8FD-30A9-46EF-916B-717A0EB9A66B Q27670418-2556F259-AF70-4E42-9CDC-6CDF4F4F642A Q27670467-0D72C006-0DDD-45E4-B2DE-65C80AF622E8 Q27671024-777B4BEA-B595-4555-A18E-A11BAD403D70 Q27674693-F5E3C5DC-9B3C-49A7-AAA3-E4E168EB40AB Q27675443-6DFA80B4-3503-4BED-A9BE-4A14691C5474 Q27675661-FEE8F665-2D87-471E-A9F5-02C0D14E9136 Q27676742-43C984B6-594C-47AA-BAFA-4111238949FB Q27677256-C05F5EE3-D44A-49D8-B855-011FF1485500 Q27677334-EEFCB06E-CA68-44FD-BEE5-6B0651A444DD Q27677869-95372709-2335-4FCE-85B4-DBCD1215FA99 Q27678108-2F195639-76C5-46DB-984F-278F18F78555 Q27678955-A22A15A3-0FD8-40FA-8B3B-38B4D9B07812 Q27680393-C4522810-9AE3-492D-942D-99C95268A556 Q27680546-8F387E03-4000-47A5-B707-91A668318FE0 Q27683690-367D771F-F118-4473-9902-564AD1CA85C4 Q27702245-E9E8855B-9152-4465-9007-0F2DEC065325 Q28237177-4BF04176-B9A0-4A23-A79F-C4E86C3C566A Q28256382-770005AC-46E6-4F7E-92EC-53E8666EF79C Q28270572-78B1CA2B-F9DF-463F-A402-8A72FD723E03 Q28270580-A2D0E8BC-AA57-4656-8E0B-39C5528E2ADD Q28273830-4CA430F0-C8B1-4C02-BCE7-D9B06D0B1418 Q28276597-FB6C9EA6-5B7F-428F-A561-5C5A2EF60B09 Q28298459-58204B9B-0E09-431C-B942-16FBCFA0D89E

P2860

Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'

http://www.wikidata.org/entity/Q27647150

description

2007 nî lūn-bûn

@nan

2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Structural evidence for a germ ...... ty complex interaction 'codon'

@ast

Structural evidence for a germ ...... ty complex interaction 'codon'

@en

Structural evidence for a germ ...... ty complex interaction 'codon'

@nl

type

label

Structural evidence for a germ ...... ty complex interaction 'codon'

@ast

Structural evidence for a germ ...... ty complex interaction 'codon'

@en

Structural evidence for a germ ...... ty complex interaction 'codon'

@nl

prefLabel

Structural evidence for a germ ...... ty complex interaction 'codon'

@ast

Structural evidence for a germ ...... ty complex interaction 'codon'

@en

Structural evidence for a germ ...... ty complex interaction 'codon'

@nl

P1433

Q27647150-49A03446-7072-4431-9E2A-0ED08FDD370C

P1476

Q27647150-59DCF34A-403F-4F8E-846C-D2AEDE327838

P2093

Q27647150-2D785213-7B7C-4DFE-B6BB-BDB9C5591633

Q27647150-71DA7380-FD0D-4E62-93DC-C0888D134061

Q27647150-7DE44478-EA8E-453F-80DA-C3B812878D77

Q27647150-81A42A72-1A5E-40D2-8AE0-DDC70AB17005

Q27647150-FEC5FE3E-CFAD-497D-8E78-A1BB4D52917B

P2860

Q27647150-05A492B9-246B-4766-B2F8-2F59417108F7

Q27647150-07BA679D-1818-4423-B5A9-675D79C97EE8

Q27647150-14101C63-4B6F-4091-93C8-02A927903BFB

Q27647150-165E5E8F-23B8-402C-96CC-584CC66A6B0F

Q27647150-1A89711E-517A-4A90-8D15-D4971F5AE90E

Q27647150-210888DD-23CE-4725-861B-D3B7D1C43157

Q27647150-23DF254B-47FA-4E2F-8080-39DD85CC5D67

Q27647150-2F6021FF-9C8E-4FF0-859A-D773AC69B69F

Q27647150-2FD78568-17DA-4812-9762-0CBBB6211D44

Q27647150-3D16C9C5-3D7D-4850-83DC-6952CB4CA1C2

P304

Q27647150-61D51475-6426-4857-9162-916D1DE44647

P31

Q27647150-570E7E6A-D26E-4B2A-AE74-7CF93F298536

P3181

Q27647150-672A0A72-77E7-4FA8-9FA6-F0C1C392DC70

P356

Q27647150-9CC67A26-223C-4A45-B636-D74C89E57073

P407

Q27647150-7A68A410-840A-495B-8802-2A9525AE3595

P433

Q27647150-2BB5F84E-C330-43B0-8FE6-B657924FFC21

P478

Q27647150-6A37060C-22A4-48CE-A85C-0D7FE225FDFF

P577

Q27647150-4696405D-FCCF-4A67-BEA1-990B618B1E25

P5875

Q27647150-603FBCA1-9BDF-4233-8527-4B2452E1640A

P698

Q27647150-CDB6291C-FBB6-49B9-8B59-3E29054FA0BA

P3181

P356

P1433

Nature Immunology

P1476

Structural evidence for a germ ...... ty complex interaction 'codon'

@en

P2093

Christopher J Bond

http://www.w3.org/2001/XMLSchema#string

Dan Feng

http://www.w3.org/2001/XMLSchema#string

Jennifer Maynard

http://www.w3.org/2001/XMLSchema#string

K Christopher Garcia

http://www.w3.org/2001/XMLSchema#string

Lauren K Ely

http://www.w3.org/2001/XMLSchema#string

P2860

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

The crystal structure of a T cell receptor in complex with peptide and MHC class II

Crystal structure of a T cell receptor bound to an allogeneic MHC molecule

Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1

A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex

A structural basis for the selection of dominant alphabeta T cell receptors in antiviral immunity

A correlation between TCR Valpha docking on MHC and CD8 dependence: implications for T cell selection

How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

How a single T cell receptor recognizes both self and foreign MHC

Structure of the complex between human T-cell receptor, viral peptide and HLA-A2

P304

975-83

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

4205792

http://www.w3.org/2001/XMLSchema#string

P356

10.1038/NI1502

http://www.w3.org/2001/XMLSchema#string

P407

P433

9

http://www.w3.org/2001/XMLSchema#string

P478

8

http://www.w3.org/2001/XMLSchema#string

P577

2007-09-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

6145601

http://www.w3.org/2001/XMLSchema#string

P698

17694060

http://www.w3.org/2001/XMLSchema#string