Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association.

Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association. Research Abstract Details 

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Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association. Abstract Text:

Gijsbert M Grotenbreg,Melissa J Nicholson,Kevin D Fowler,Kathrin Wilbuer,Leah Octavio,Maxine Yang,Arup K Chakraborty,Hidde L Ploegh,Kai W Wucherpfennig,

DM catalyzes the exchange of peptides bound to Class II major histocompatibility complex (MHC) molecules. Because the dissociation and association components of the overall reaction are difficult to separate, a detailed mechanism of DM catalysis has long resisted elucidation. UV irradiation of DR molecules loaded with a photocleavable peptide (caged Class II MHC molecules) enabled synchronous and verifiable evacuation of the peptide-binding groove and tracking of early binding events in real time by fluorescence polarization. Empty DR molecules generated by photocleavage rapidly bound peptide but quickly resolved into species with substantially slower binding kinetics. DM formed a complex with empty DR molecules that bound peptide with even faster kinetics than empty DR molecules just having lost their peptide cargo. Mathematical models demonstrate that the peptide association rate of DR molecules is substantially higher in the presence of DM. We therefore unequivocally establish that DM contributes directly to peptide association through formation of a peptide-loading complex between DM and empty Class II MHC. This complex rapidly acquires a peptide analogous to the MHC class I peptide-loading complex.

Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association. Publishing Authors By Initials

GM Grotenbreg,MJ Nicholson,KD Fowler,K Wilbuer,L Octavio,M Yang,AK Chakraborty,HL Ploegh,KW Wucherpfennig,

For similar environment and public health: environment: meteorological factors: atmosphere: weather: sunlight: ultraviolet rays research abstracts see: environment and public health: environment: meteorological factors: atmosphere: weather: sunlight: ultraviolet rays research

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Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 21425-36

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 24

MONTH: 05

YEAR: 2007

Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association. Keywords Mesh Terms:

KEYWORDS: Ultraviolet Rays

MESH TERMS: methods

Chemical & Substance for Abstract: Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association. Information

Substance Name: Peptides

Registry Number: 0

Grant and Affiliation Information for Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association.

AFFILIATION: Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02139, USA.

Country: United States

AGENCY: United States NIAID

GRANT: R01 AI057493

ACRONYM: AI

MEDLINETA: J Biol Chem

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