| A structural and molecular dynamics approach to understanding the peptide-receptive transition state of MHC-I molecules. | |
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MedLine Citation:
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PMID: 23200143 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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The mature conformation of major histocompatibility complex class I (MHC-I) proteins depends on the presence of bound peptides, permitting recognition at the cell surface by CD8(+) T lymphocytes. Newly synthesized MHC-I molecules in the endoplasmic reticulum are maintained in a peptide-receptive (PR) transition state by several chaperones until they are released concomitant with the loading of peptides. By determining the crystallographic structure of a region of an MHC-I molecule that is recognized by a unique monoclonal antibody and comparing this with docking and molecular dynamics simulations with the whole molecule, we demonstrate the movement of a hinged unit supporting the part of the binding groove that interacts with the amino terminal residues of the bound peptide. This unit contains a conserved 3(10) helix that flips from an exposed "open" position in the PR form to a "closed" position in the peptide-loaded (PL) mature molecule. These analyses indicate how this segment of the MHC-I molecule moves to help establish the A and B pockets critical for tight peptide binding and the stable structure required for antigen presentation and T cell recognition at the cell surface. |
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Authors:
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Michael G Mage; Michael A Dolan; Rui Wang; Lisa F Boyd; Maria Jamela Revilleza; Howard Robinson; Kannan Natarajan; Nancy B Myers; Ted H Hansen; David H Margulies |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-11-28 |
Journal Detail:
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Title: Molecular immunology Volume: - ISSN: 1872-9142 ISO Abbreviation: Mol. Immunol. Publication Date: 2012 Nov |
Date Detail:
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Created Date: 2012-12-3 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7905289 Medline TA: Mol Immunol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Published by Elsevier Ltd. |
Affiliation:
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Molecular Biology Section, Laboratory of Immunology, NIAID, NIH, Bethesda, MD 20892, USA. Electronic address: mmage@mail.nih.gov. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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