Abstract
We describe the X-ray crystallographic structure of a murine T cell receptor (TCR) Vα domain ("Vα85.33"; AV11S5-AJ17) to 1.85 Å resolution. The Vα85.33 domain is derived from a TCR that recognizes a type II collagen peptide associated with the murine major histocompatibility complex (MHC) class II molecule, I-Aq. Vα85.33 packs as a Vα-Vα homodimer with a highly symmetric monomer-monomer interface. The first and second complementarity determining regions (CDR1 and CDR2) of this Vα are shorter than the CDRs corresponding to the majority of other Vα gene families, and three-dimensional structures of CDRs of these lengths have not been described previously. The CDR1 and CDR2 therefore represent new canonical forms that could serve as templates for AV11 family members. CDR3 of the Vα85.33 domain is highly flexible and this is consistent with plasticity of this region of the TCR. The fourth hypervariable loop (HV4α) of AV11 and AV10 family members is one residue longer than that of other HV4α regions and shows a high degree of flexibility. The increase in length results in a distinct disposition of the conserved residue Lys68, which has been shown in other studies to play a role in antigen recognition. The X-ray structure of Vα85.33 extends the database of canonical forms for CDR1 and CDR2, and has implications for antigen recognition by TCRs that contain related Vα domains.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 689-698 |
| Number of pages | 10 |
| Journal | Journal of Molecular Biology |
| Volume | 310 |
| Issue number | 4 |
| DOIs | |
| State | Published - Jul 20 2001 |
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Keywords
- Antigen recognition
- Canonical form
- Complementarity determining region
- T cell receptor Vα domain
- X-ray crystallography
ASJC Scopus subject areas
- Virology
Cite this
Crystal structure of a T cell receptor Vα11 (AV11S5) domain : New canonical forms for the first and second complementarity determining regions. / Machius, Mischa; Cianga, Petru; Deisenhofer, Johann; Ward, E. Sally.
In: Journal of Molecular Biology, Vol. 310, No. 4, 20.07.2001, p. 689-698.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystal structure of a T cell receptor Vα11 (AV11S5) domain
T2 - New canonical forms for the first and second complementarity determining regions
AU - Machius, Mischa
AU - Cianga, Petru
AU - Deisenhofer, Johann
AU - Ward, E. Sally
PY - 2001/7/20
Y1 - 2001/7/20
N2 - We describe the X-ray crystallographic structure of a murine T cell receptor (TCR) Vα domain ("Vα85.33"; AV11S5-AJ17) to 1.85 Å resolution. The Vα85.33 domain is derived from a TCR that recognizes a type II collagen peptide associated with the murine major histocompatibility complex (MHC) class II molecule, I-Aq. Vα85.33 packs as a Vα-Vα homodimer with a highly symmetric monomer-monomer interface. The first and second complementarity determining regions (CDR1 and CDR2) of this Vα are shorter than the CDRs corresponding to the majority of other Vα gene families, and three-dimensional structures of CDRs of these lengths have not been described previously. The CDR1 and CDR2 therefore represent new canonical forms that could serve as templates for AV11 family members. CDR3 of the Vα85.33 domain is highly flexible and this is consistent with plasticity of this region of the TCR. The fourth hypervariable loop (HV4α) of AV11 and AV10 family members is one residue longer than that of other HV4α regions and shows a high degree of flexibility. The increase in length results in a distinct disposition of the conserved residue Lys68, which has been shown in other studies to play a role in antigen recognition. The X-ray structure of Vα85.33 extends the database of canonical forms for CDR1 and CDR2, and has implications for antigen recognition by TCRs that contain related Vα domains.
AB - We describe the X-ray crystallographic structure of a murine T cell receptor (TCR) Vα domain ("Vα85.33"; AV11S5-AJ17) to 1.85 Å resolution. The Vα85.33 domain is derived from a TCR that recognizes a type II collagen peptide associated with the murine major histocompatibility complex (MHC) class II molecule, I-Aq. Vα85.33 packs as a Vα-Vα homodimer with a highly symmetric monomer-monomer interface. The first and second complementarity determining regions (CDR1 and CDR2) of this Vα are shorter than the CDRs corresponding to the majority of other Vα gene families, and three-dimensional structures of CDRs of these lengths have not been described previously. The CDR1 and CDR2 therefore represent new canonical forms that could serve as templates for AV11 family members. CDR3 of the Vα85.33 domain is highly flexible and this is consistent with plasticity of this region of the TCR. The fourth hypervariable loop (HV4α) of AV11 and AV10 family members is one residue longer than that of other HV4α regions and shows a high degree of flexibility. The increase in length results in a distinct disposition of the conserved residue Lys68, which has been shown in other studies to play a role in antigen recognition. The X-ray structure of Vα85.33 extends the database of canonical forms for CDR1 and CDR2, and has implications for antigen recognition by TCRs that contain related Vα domains.
KW - Antigen recognition
KW - Canonical form
KW - Complementarity determining region
KW - T cell receptor Vα domain
KW - X-ray crystallography
UR - http://www.scopus.com/inward/record.url?scp=0035919777&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035919777&partnerID=8YFLogxK
U2 - 10.1006/jmbi.2001.4794
DO - 10.1006/jmbi.2001.4794
M3 - Article
C2 - 11453680
AN - SCOPUS:0035919777
VL - 310
SP - 689
EP - 698
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 4
ER -