5ib3 | pdb_00005ib3

Crystal structure of HLA-B*27:05 complexed with the self-peptide pVIPR and Copper

spinqualitylabelsall models 5ib3, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ib3 is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.91Å Ligands: CU, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function VIPR1_HUMAN This is a receptor for VIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The affinity is VIP = PACAP-27 > PACAP-38. Publication Abstract from PubMed Conformational changes of major histocompatibility complex (MHC) antigens have the potential to be recognized by T cells and may arise from polymorphic variation of the MHC molecule, the binding of modifying ligands, or both. Here, we investigated whether metal ions could affect allele-dependent structural variation of the two minimally distinct human leukocyte antigen (HLA)-B*27:05 and HLA-B*27:09 subtypes, which exhibit differential association with the rheumatic disease ankylosing spondylitis (AS). We employed NMR spectroscopy and X-ray crystallography coupled with ensemble refinement to study the AS-associated HLA-B*27:05 subtype and the AS non-associated HLA-B* 27:09 in complex with the self-peptide pVIPR (RRKWRRWHL). Both techniques revealed that pVIPR exhibits a higher degree of flexibility when complexed with HLA-B* 27:05 than with HLA-B*27:09. Furthermore, we found that the binding of the metal ions Cu2+ or Ni2+, but not Mn2+, Zn2+, or Hg2+ affects the structure of a pVIPR-bound HLA-B*27 molecule in a subtype-dependent manner. In HLA-B*27:05, the metals triggered conformational reorientations of pVIPR, but no such structural changes were observed in the HLA-B*27:09 subtype, with or without bound metal ion. These observations provide the first demonstration that not only MHC class II, but also class I molecules can undergo metal ion-induced conformational alterations. Our findings suggest that metals may have role in triggering rheumatic diseases such as AS and also have implications for the molecular basis of metal-induced hypersensitivities and allergies. Metal-triggered conformational reorientation of a self-peptide bound to a disease-associated HLA-B*27 subtype.,Driller R, Ballaschk M, Schmieder P, Uchanska-Ziegler B, Ziegler A, Loll B J Biol Chem. 2019 Jul 11. pii: RA119.008937. doi: 10.1074/jbc.RA119.008937. PMID:31296658 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-2 microglobulin 3D structures MHC 3D structures MHC I 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA