3LN5

Crystal structure of HLA-B*4104 in complex with a 11mer self-peptide derived from S-methyl-5-thioadenosine phosphorylase

Summary for 3LN5

• Entry DOI: 10.2210/pdb3ln5/pdb
• Related: 3LN4
• Descriptor: HLA class I histocompatibility antigen, B-41 alpha chain, Beta-2-microglobulin, 11-mer peptide from S-methyl-5'-thioadenosine phosphorylase, ... (4 entities in total)
• Functional Keywords: immunoglobulin domain, immune response, major histocompatibility complex class i, mhc-i peptide complex, peptide-binding motifs, disulfide bond, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P30479; Secreted: P61769; Cytoplasm: Q13126
• Total number of polymer chains: 3
• Total formula weight: 44775.50

Authors

Theodossis, A.,Gras, S.,Rossjohn, J. (deposition date: 2010-02-02, release date: 2010-10-20, Last modification date: 2024-11-06)

Primary citation

Bade-Doding, C.,Theodossis, A.,Gras, S.,Kjer-Nielsen, L.,Eiz-Vesper, B.,Seltsam, A.,Huyton, T.,Rossjohn, J.,McCluskey, J.,Blasczyk, R.
The impact of human leukocyte antigen (HLA) micropolymorphism on ligand specificity within the HLA-B*41 allotypic family
Haematologica, 96:110-118, 2011

PubMed Abstract: Polymorphic differences between human leukocyte antigen (HLA) molecules affect the specificity and conformation of their bound peptides and lead to differential selection of the T-cell repertoire. Mismatching during allogeneic transplantation can, therefore, lead to immunological reactions.

PubMed: 20934997
DOI: 10.3324/haematol.2010.030924

Experimental method

X-RAY DIFFRACTION (1.9 Å)