6a97: Difference between revisions
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The | ==Crystal structure of MHC-like MILL2== | ||
<StructureSection load='6a97' size='340' side='right' caption='[[6a97]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6a97]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A97 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A97 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6a97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a97 OCA], [http://pdbe.org/6a97 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a97 RCSB], [http://www.ebi.ac.uk/pdbsum/6a97 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a97 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/B2MG_MOUSE B2MG_MOUSE]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The MILL family, composed of MILL1 and MILL2, is a group of nonclassical MHC class I molecules that occur in some orders of mammals. It has been reported that mouse MILL2 is involved in wound healing; however, the molecular mechanisms remain unknown. Here, we determine the crystal structure of MILL2 at 2.15 A resolution, revealing an organization similar to classical MHC class I. However, the alpha1-alpha2 domains are not tightly fixed on the alpha3-beta2m domains, indicating unusual interdomain flexibility. The groove between the two helices in the alpha1-alpha2 domains is too narrow to permit ligand binding. Notably, an unusual basic patch on the alpha3 domain is involved in the binding to heparan sulfate which is essential for MILL2 interactions with fibroblasts. These findings suggest that MILL2 has a unique structural architecture and physiological role, with binding to heparan sulfate proteoglycans on fibroblasts possibly regulating cellular recruitment in biological events. | |||
Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility.,Kajikawa M, Ose T, Fukunaga Y, Okabe Y, Matsumoto N, Yonezawa K, Shimizu N, Kollnberger S, Kasahara M, Maenaka K Nat Commun. 2018 Oct 18;9(1):4330. doi: 10.1038/s41467-018-06797-8. PMID:30337538<ref>PMID:30337538</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6a97" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Kajikawa, M]] | [[Category: Kajikawa, M]] | ||
[[Category: Maenaka, K]] | |||
[[Category: Ose, T]] | [[Category: Ose, T]] | ||
[[Category: | [[Category: Immune system]] | ||
[[Category: Mhc-like]] | |||
Revision as of 09:31, 5 December 2018
Crystal structure of MHC-like MILL2Crystal structure of MHC-like MILL2
Structural highlights
Function[B2MG_MOUSE] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Publication Abstract from PubMedThe MILL family, composed of MILL1 and MILL2, is a group of nonclassical MHC class I molecules that occur in some orders of mammals. It has been reported that mouse MILL2 is involved in wound healing; however, the molecular mechanisms remain unknown. Here, we determine the crystal structure of MILL2 at 2.15 A resolution, revealing an organization similar to classical MHC class I. However, the alpha1-alpha2 domains are not tightly fixed on the alpha3-beta2m domains, indicating unusual interdomain flexibility. The groove between the two helices in the alpha1-alpha2 domains is too narrow to permit ligand binding. Notably, an unusual basic patch on the alpha3 domain is involved in the binding to heparan sulfate which is essential for MILL2 interactions with fibroblasts. These findings suggest that MILL2 has a unique structural architecture and physiological role, with binding to heparan sulfate proteoglycans on fibroblasts possibly regulating cellular recruitment in biological events. Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility.,Kajikawa M, Ose T, Fukunaga Y, Okabe Y, Matsumoto N, Yonezawa K, Shimizu N, Kollnberger S, Kasahara M, Maenaka K Nat Commun. 2018 Oct 18;9(1):4330. doi: 10.1038/s41467-018-06797-8. PMID:30337538[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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