3bev: Difference between revisions

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[[Image:3bev.png|left|200px]]


{{STRUCTURE_3bev| PDB=3bev | SCENE= }}
==11mer Structure of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding==
<StructureSection load='3bev' size='340' side='right'caption='[[3bev]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3bev]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BEV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bev OCA], [https://pdbe.org/3bev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bev RCSB], [https://www.ebi.ac.uk/pdbsum/3bev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bev ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q95601_CHICK Q95601_CHICK]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/be/3bev_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bev ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Little is known about the structure of major histocompatibility complex (MHC) molecules outside of mammals. Only one class I molecule in the chicken MHC is highly expressed, leading to strong genetic associations with infectious pathogens. Here, we report two structures of the MHC class I molecule BF2*2101 from the B21 haplotype, which is known to confer resistance to Marek's disease caused by an oncogenic herpesvirus. The binding groove has an unusually large central cavity, which confers substantial conformational flexibility to the crucial residue Arg9, allowing remodeling of key peptide-binding sites. The coupled variation of anchor residues from the peptide, utilizing a charge-transfer system unprecedented in MHC molecules, allows peptides with conspicuously different sequences to be bound. This promiscuous binding extends our understanding of ways in which MHC class I molecules can present peptides to the immune system and might explain the resistance of the B21 haplotype to Marek's disease.


===11mer Structure of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding===
Structures of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding.,Koch M, Camp S, Collen T, Avila D, Salomonsen J, Wallny HJ, van Hateren A, Hunt L, Jacob JP, Johnston F, Marston DA, Shaw I, Dunbar PR, Cerundolo V, Jones EY, Kaufman J Immunity. 2007 Dec;27(6):885-99. PMID:18083574<ref>PMID:18083574</ref>


{{ABSTRACT_PUBMED_18083574}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 3bev" style="background-color:#fffaf0;"></div>
[[3bev]] is a 3 chain structure of [[Beta-2 microglobulin]], [[Hemoglobin]] and [[Major histocompatibility complex]] with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BEV OCA].


==See Also==
==See Also==
*[[Beta-2 microglobulin|Beta-2 microglobulin]]
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
*[[Hemoglobin|Hemoglobin]]
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
*[[Major histocompatibility complex|Major histocompatibility complex]]
*[[MHC 3D structures|MHC 3D structures]]
 
*[[MHC I 3D structures|MHC I 3D structures]]
==Reference==
== References ==
<ref group="xtra">PMID:018083574</ref><references group="xtra"/>
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Jones, Y.]]
[[Category: Large Structures]]
[[Category: Kaufman, J.]]
[[Category: Jones Y]]
[[Category: Koch, M.]]
[[Category: Kaufman J]]
[[Category: 11mer]]
[[Category: Koch M]]
[[Category: B21]]
[[Category: Bf21]]
[[Category: Bulge]]
[[Category: Chicken]]
[[Category: Heme]]
[[Category: Immune response]]
[[Category: Immune system]]
[[Category: Immunoglobulin domain]]
[[Category: Iron]]
[[Category: Metal-binding]]
[[Category: Mhc class i]]
[[Category: Mhc i]]
[[Category: Oxygen transport]]
[[Category: Secreted]]
[[Category: Transport]]
[[Category: Water cushion]]

Latest revision as of 04:37, 21 November 2024

11mer Structure of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding11mer Structure of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding

Structural highlights

3bev is a 3 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q95601_CHICK

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Little is known about the structure of major histocompatibility complex (MHC) molecules outside of mammals. Only one class I molecule in the chicken MHC is highly expressed, leading to strong genetic associations with infectious pathogens. Here, we report two structures of the MHC class I molecule BF2*2101 from the B21 haplotype, which is known to confer resistance to Marek's disease caused by an oncogenic herpesvirus. The binding groove has an unusually large central cavity, which confers substantial conformational flexibility to the crucial residue Arg9, allowing remodeling of key peptide-binding sites. The coupled variation of anchor residues from the peptide, utilizing a charge-transfer system unprecedented in MHC molecules, allows peptides with conspicuously different sequences to be bound. This promiscuous binding extends our understanding of ways in which MHC class I molecules can present peptides to the immune system and might explain the resistance of the B21 haplotype to Marek's disease.

Structures of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding.,Koch M, Camp S, Collen T, Avila D, Salomonsen J, Wallny HJ, van Hateren A, Hunt L, Jacob JP, Johnston F, Marston DA, Shaw I, Dunbar PR, Cerundolo V, Jones EY, Kaufman J Immunity. 2007 Dec;27(6):885-99. PMID:18083574[1]

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

See Also

References

  1. Koch M, Camp S, Collen T, Avila D, Salomonsen J, Wallny HJ, van Hateren A, Hunt L, Jacob JP, Johnston F, Marston DA, Shaw I, Dunbar PR, Cerundolo V, Jones EY, Kaufman J. Structures of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding. Immunity. 2007 Dec;27(6):885-99. PMID:18083574 doi:10.1016/j.immuni.2007.11.007

3bev, resolution 2.10Å

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