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| - | [[Image:1k8d.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1k8d| PDB=1k8d | SCENE= }} | | {{STRUCTURE_1k8d| PDB=1k8d | SCENE= }} |
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| - | '''crystal structure of the non-classical MHC class Ib Qa-2 complexed with a self peptide'''
| + | ===crystal structure of the non-classical MHC class Ib Qa-2 complexed with a self peptide=== |
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| - | ==Overview==
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| - | BACKGROUND: Qa-2 is a nonclassical MHC Ib antigen, which has been implicated in both innate and adaptive immune responses, as well as embryonic development. Qa-2 has an unusual peptide binding specificity in that it requires two dominant C-terminal anchor residues and is capable of associating with a substantially more diverse array of peptide sequences than other nonclassical MHC. RESULTS: We have determined the crystal structure, to 2.3 A, of the Q9 gene of murine Qa-2 complexed with a self-peptide derived from the L19 ribosomal protein, which is abundant in the pool of peptides eluted from the Q9 groove. The 9 amino acid peptide is bound high in a shallow, hydrophobic binding groove of Q9, which is missing a C pocket. The peptide makes few specific contacts and exhibits extremely poor shape complementarity to the MHC groove, which facilitates the presentation of a degenerate array of sequences. The L19 peptide is in a centrally bulged conformation that is stabilized by intramolecular interactions from the invariant P7 histidine anchor residue and by a hydrophobic core of preferred secondary anchor residues that have minimal interaction with the MHC. CONCLUSIONS: Unexpectedly, the preferred secondary peptide residues that exhibit tenuous contact with Q9 contribute significantly to the overall stability of the peptide-MHC complex. The structure of this complex implies a "conformational" selection by Q9 for peptide residues that optimally stabilize the large bulge rather than making intimate contact with the MHC pockets.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11738047}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11738047 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11738047}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Q9]] | | [[Category: Q9]] |
| | [[Category: Qa-2]] | | [[Category: Qa-2]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:25:46 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 09:56:25 2008'' |
Revision as of 06:56, 2 July 2008
Template:STRUCTURE 1k8d
crystal structure of the non-classical MHC class Ib Qa-2 complexed with a self peptide
Template:ABSTRACT PUBMED 11738047
About this Structure
1K8D is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Promiscuous antigen presentation by the nonclassical MHC Ib Qa-2 is enabled by a shallow, hydrophobic groove and self-stabilized peptide conformation., He X, Tabaczewski P, Ho J, Stroynowski I, Garcia KC, Structure. 2001 Dec;9(12):1213-24. PMID:11738047
Page seeded by OCA on Wed Jul 2 09:56:25 2008
