1ld9: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1ld9.gif|left|200px]]
{{Seed}}
[[Image:1ld9.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ld9|  PDB=1ld9  |  SCENE=  }}  
{{STRUCTURE_1ld9|  PDB=1ld9  |  SCENE=  }}  


'''THE THREE-DIMENSIONAL STRUCTURE OF AN H-2LD PEPTIDE COMPLEX EXPLAINS THE UNIQUE INTERACTION OF LD WITH BETA2M AND PEPTIDE'''
===THE THREE-DIMENSIONAL STRUCTURE OF AN H-2LD PEPTIDE COMPLEX EXPLAINS THE UNIQUE INTERACTION OF LD WITH BETA2M AND PEPTIDE===




==Overview==
<!--  
Solution at 2.5-A resolution of the three-dimensional structure of H-2Ld with a single nine-residue peptide provides a structural basis for understanding its unique interaction with beta-2 microglobulin (beta2m) and peptide. Consistent with the biological data that show an unusually weak association of Ld with beta2m, a novel orientation of the alpha1/alpha2 domains of Ld relative to beta2m results in a dearth of productive contacts compared with other class I proteins. Characteristics of the Ld antigen-binding cleft determine the unique motif of peptides that it binds. Ld has no central anchor residue due to the presence of several bulky side chains in its mid-cleft region. Also, its cleft is significantly more hydrophobic than that of the other class I molecules for which structures are known, resulting in many fewer H-bonds between peptide and cleft residues. The choice of Pro as a consensus anchor at peptide position 2 appears to be related to the hydrophobicity of the B pocket, and to the unique occurrence of Ile (which mirrors Pro in its inability to form H-bonds) at position 63 on the edge of this pocket. Thus, the paucity of stabilizing H-bonds combined with poor complementarity between peptide postion 2 Pro and the B pocket contribute to the weak association between Ld and its peptide antigen. The unique structural interactions of Ld with beta2m and peptide could make Ld more suited than other classical class I molecules to play a role in alternative pathways of antigen presentation.
The line below this paragraph, {{ABSTRACT_PUBMED_9192660}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9192660 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_9192660}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Ld]]
[[Category: Ld]]
[[Category: Major histocompatibility complex]]
[[Category: Major histocompatibility complex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:48:32 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:29:46 2008''

Revision as of 09:29, 2 July 2008

File:1ld9.png

Template:STRUCTURE 1ld9

THE THREE-DIMENSIONAL STRUCTURE OF AN H-2LD PEPTIDE COMPLEX EXPLAINS THE UNIQUE INTERACTION OF LD WITH BETA2M AND PEPTIDE

Template:ABSTRACT PUBMED 9192660

About this Structure

1LD9 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

The three-dimensional structure of an H-2Ld-peptide complex explains the unique interaction of Ld with beta-2 microglobulin and peptide., Balendiran GK, Solheim JC, Young AC, Hansen TH, Nathenson SG, Sacchettini JC, Proc Natl Acad Sci U S A. 1997 Jun 24;94(13):6880-5. PMID:9192660

Page seeded by OCA on Wed Jul 2 12:29:46 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1ld9&oldid=625019"