2BC4,1HDM,1K8I


Conserved Protein Domain Family
IgC1_MHC_II_alpha_HLA-DM

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cd21009: IgC1_MHC_II_alpha_HLA-DM 
Class II major histocompatibility complex (MHC) alpha chain immunoglobulin domain of histocompatibility antigen (HLA) DM; member of the C1-set of Ig superfamily (IgSF) domains
The members here are composed of the immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class II alpha chain of histocompatibility antigen (HLA) DM. Human HLA-DM, also known as H2-M in mice, plays a critical role in antigen presentation to CD4 T cells by catalyzing the exchange of peptides bound to MHC class II molecules. MHC class II molecules play a key role in the initiation of the antigen-specific immune reponse. These molecules have been shown to be expressed constitutively on the cell surface of professional antigen-presenting cells (APCs), including B-lymphocytes, monocytes, and macrophages in both humans and mice. The expression of these molecules has been shown to be induced in nonprofessional APCs such as keratinocyctes, and they are expressed on the surface of activated human T cells and on T cells from other species. The MHC II molecules present antigenic peptides to CD4(+) T-lymphocytes. These peptides derive mostly from proteolytic processing via the endocytic pathway, of antigens internalized by the APC. These peptides bind to the MHC class II molecules in the endosome before they are transported to the cell surface. MHC class II molecules are heterodimers, comprised of two similarly-sized membrane-spanning chains, alpha and beta. Each chain had two globular domains (N- and C-terminal), and a membrane-anchoring transmembrane segment. The two chains form a compact four-domain structure. The peptide-binding site is a cleft in the structure.
Statistics
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PSSM-Id: 409600
Aligned: 5 rows
Threshold Bit Score: 185.628
Created: 13-Mar-2019
Updated: 25-Oct-2021
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 7 residues -Click on image for an interactive view with Cn3D
Feature 1:heterodimer interface [polypeptide binding site]
Evidence:
  • Comment:Dimerization of IgC domains from different chains is common, but not found in all members.
  • Structure:1HDM; human class II histocompatibility antigen (HLA-DM), alpha/beta chain interface between IgC domains, based on 3.5 A distance.
    View structure with Cn3D
  • Citation:PMID 9768757

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1          # ### #                                                  # #               
2BC4_A     99 GFPIAEVFTLKPLEFGKPNTLVCFVSNLFPPMLTVNWQHHSVPVEGFGPTFVSAVDGLSFQAFSYLNFTPEPSDIFSCIV 178 human
1HDM_A     96 GFPIAEVFTLKPLEFGKPNTLVCFVSNLFPPMLTVNWHDHSVPVEGFGPTFVSAVDGLSFQAFSYLNFTPEPSDIFSCIV 175 human
P28067    125 GFPIAEVFTLKPLEFGKPNTLVCFVSNLFPPMLTVNWHDHSVPVEGFGPTFVSAVDGLSFQAFSYLNFTPEPSDIFSCIV 204 human
P28078    125 GLSVAEVFTLKPLEFGKPNTLVCFISNLFPPTLTVNWQLHSAPVEGASPTSISAVDGLTFQAFSYLNFTPEPFDLYSCTV 204 house mouse
1K8I_A     96 GLPVAEVFTLKPLEFGKPNTLVCFISNLFPPTLTVNWQLHSAPVEGASPTSISAVDGLTFQAFSYLNFTPEPFDLYSCTV 175 house mouse
Feature 1                   
2BC4_A    179 THEIDRYTAIAYWV 192 human
1HDM_A    176 THEPDRYTAIAYWV 189 human
P28067    205 THEIDRYTAIAYWV 218 human
P28078    205 THEIDRYTAIAYWV 218 house mouse
1K8I_A    176 THEIDRYTAIAYWV 189 house mouse

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