3bev: Difference between revisions

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==See Also==
==See Also==
*[[Beta-2 microglobulin|Beta-2 microglobulin]]
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
*[[Major histocompatibility complex|Major histocompatibility complex]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Mhc i]]
[[Category: Mhc i]]
[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
[[Category: Polymorphism]]
[[Category: Secreted]]
[[Category: Secreted]]
[[Category: Transport]]
[[Category: Transport]]
[[Category: Water cushion]]
[[Category: Water cushion]]

Revision as of 11:01, 25 October 2017

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 Chick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:BFIV21, B-FIV, BF2 (CHICK), B2M (CHICK)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HBA_CHICK] Involved in oxygen transport from the lung to the various peripheral tissues. [B2MG_CHICK] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.

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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OCA