Crystal structure of a T cell receptor Vα11 (AV11S5) domain:: New canonical forms for the first and second complementarity determining regions
Crystal structure of a T cell receptor Vα11 (AV11S5) domain:: New canonical forms for the first and second complementarity determining regions
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DOI：
10.1006/jmbi.2001.4794
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发表时间：
2001-07-20
影响因子：
5.6
通讯作者：
Ward, ES
中科院分区：
文献类型：
--
作者：
Machius, M;Cianga, P;Ward, ES
我们描述了鼠T细胞受体（TCR）V α结构域（“V α 85.33“; AV 11 S5-AJ17）的X射线晶体结构，分辨率为1.85埃。V α 85.33结构域来源于TCR，其识别与鼠主要组织相容性复合体（MHC）II类分子I-A（q）相关的II型胶原肽。V α 85.33包装为具有高度对称的单体-单体界面的V α-V α同二聚体。该Ver的第一和第二互补决定区（CDR 1和CDR 2）比对应于大多数其它V α基因家族的CDR短，并且这些长度的CDR的三维结构先前未被描述。因此，CDR 1和CDR 2代表了新的规范形式，可以作为AV 11家族成员的模板。V α 85.33结构域的CDR 3是高度柔性的，这与TCR的该区域的可塑性一致。AV 11和AV 10家族成员的第四个高变环（HV 4 α）比其他HV 4 α区长一个残基，并显示出高度的灵活性。长度的增加导致保守残基Lys 68的独特处置，其已在其他研究中显示在抗原识别中起作用。V α 85.33的X射线结构扩展了CDR 1和CDR 2的规范形式的数据库，并对含有相关Vex结构域的TCR的抗原识别具有影响。(C)北京：科学出版社.
We describe the X-ray crystallographic structure of a murine T cell receptor (TCR) V alpha domain ("V alpha 85.33 "; AV11S5-AJ17) to 1.85 Angstrom resolution. The V alpha 85.33 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-A(q). V alpha 85.33 packs as a V alpha -V alpha homodimer with a highly symmetric monomer-monomer interface. The first and second complementarity determining regions (CDR1 and CDR2) of this Ver are shorter than the CDRs corresponding to the majority of other V alpha 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 V alpha 85.33 domain is highly flexible and this is consistent with plasticity of this region of the TCR. The fourth hypervariable loop (HV4 alpha) of AV11 and AV10 family members is one residue longer than that of other HV4 alpha 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 V alpha 85.33 extends the database of canonical forms for CDR1 and CDR2, and has implications for antigen recognition by TCRs that contain related Vex domains. (C) 2001 Academic Press.