7tud: Difference between revisions

Latest revision as of 11:42, 30 October 2024

Crystal structure of HLA-B*44:05 (T73C) with 6mer EEFGRC and dipeptide GL

Structural highlights

7tud is a 4 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.45Å
Ligands:	EDO, GOL
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

D5H3J5_HUMAN

Publication Abstract from PubMed

Loading of MHC-I molecules with peptide by the catalytic chaperone tapasin in the peptide loading complex plays a critical role in antigen presentation and immune recognition. Mechanistic insight has been hampered by the lack of detailed structural information concerning tapasin-MHC-I. We present here crystal structures of human tapasin complexed with the MHC-I molecule HLA-B*44:05, and with each of two anti-tapasin antibodies. The tapasin-stabilized peptide-receptive state of HLA-B*44:05 is characterized by distortion of the peptide binding groove and destabilization of the beta(2)-microglobulin interaction, leading to release of peptide. Movements of the membrane proximal Ig-like domains of tapasin, HLA-B*44:05, and beta(2)-microglobulin accompany the transition to a peptide-receptive state. Together this ensemble of crystal structures provides insights into a distinct mechanism of tapasin-mediated peptide exchange.

Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation.,Jiang J, Taylor DK, Kim EJ, Boyd LF, Ahmad J, Mage MG, Truong HV, Woodward CH, Sgourakis NG, Cresswell P, Margulies DH, Natarajan K Nat Commun. 2022 Sep 17;13(1):5470. doi: 10.1038/s41467-022-33153-8. PMID:36115831^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jiang J, Taylor DK, Kim EJ, Boyd LF, Ahmad J, Mage MG, Truong HV, Woodward CH, Sgourakis NG, Cresswell P, Margulies DH, Natarajan K. Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation. Nat Commun. 2022 Sep 17;13(1):5470. PMID:36115831 doi:10.1038/s41467-022-33153-8

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Jiang J, Taylor DK, Kim EJ, Boyd LF, Ahmad J, Mage MG, Truong HV, Woodward CH, Sgourakis NG, Cresswell P, Margulies DH, Natarajan K. Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation. Nat Commun. 2022 Sep 17;13(1):5470. PMID:36115831 doi:10.1038/s41467-022-33153-8

[1]

@@ Line 8: / Line 8: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7tud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tud OCA], [https://pdbe.org/7tud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tud RCSB], [https://www.ebi.ac.uk/pdbsum/7tud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tud ProSAT]</span></td></tr>
 </table>
-== Disease ==
-[https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[https://omim.org/entry/241600 241600]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref>   Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref> <ref>PMID:1336137</ref> <ref>PMID:7554280</ref> <ref>PMID:4586824</ref> <ref>PMID:8084451</ref> <ref>PMID:12119416</ref> <ref>PMID:12796775</ref> <ref>PMID:16901902</ref> <ref>PMID:16491088</ref> <ref>PMID:17646174</ref> <ref>PMID:18835253</ref> <ref>PMID:18395224</ref> <ref>PMID:19284997</ref>
 == Function ==
-[https://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
+[https://www.uniprot.org/uniprot/D5H3J5_HUMAN D5H3J5_HUMAN]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Loading of MHC-I molecules with peptide by the catalytic chaperone tapasin in the peptide loading complex plays a critical role in antigen presentation and immune recognition. Mechanistic insight has been hampered by the lack of detailed structural information concerning tapasin-MHC-I. We present here crystal structures of human tapasin complexed with the MHC-I molecule HLA-B*44:05, and with each of two anti-tapasin antibodies. The tapasin-stabilized peptide-receptive state of HLA-B*44:05 is characterized by distortion of the peptide binding groove and destabilization of the beta(2)-microglobulin interaction, leading to release of peptide. Movements of the membrane proximal Ig-like domains of tapasin, HLA-B*44:05, and beta(2)-microglobulin accompany the transition to a peptide-receptive state. Together this ensemble of crystal structures provides insights into a distinct mechanism of tapasin-mediated peptide exchange.
+Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation.,Jiang J, Taylor DK, Kim EJ, Boyd LF, Ahmad J, Mage MG, Truong HV, Woodward CH, Sgourakis NG, Cresswell P, Margulies DH, Natarajan K Nat Commun. 2022 Sep 17;13(1):5470. doi: 10.1038/s41467-022-33153-8. PMID:36115831<ref>PMID:36115831</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 7tud" style="background-color:#fffaf0;"></div>
 ==See Also==

7tud: Difference between revisions

Latest revision as of 11:42, 30 October 2024

Crystal structure of HLA-B*44:05 (T73C) with 6mer EEFGRC and dipeptide GL

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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