This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3hla

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3hla.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3hla.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3hla| PDB=3hla | SCENE= }}
{{STRUCTURE_3hla| PDB=3hla | SCENE= }}
-
'''SPECIFICITY POCKETS FOR THE SIDE CHAINS OF PEPTIDE ANTIGENS IN HLA-AW68'''
+
===SPECIFICITY POCKETS FOR THE SIDE CHAINS OF PEPTIDE ANTIGENS IN HLA-AW68===
-
==Overview==
+
<!--
-
The three-dimensional structure of the human histocompatibility antigen HLA-A2 was determined at 3.5 A resolution by a combination of isomorphous replacement and iterative real-space averaging of two crystal forms. The monoclinic crystal form has now been refined by least-squares methods to an R-factor of 0.169 for data from 6 to 2.6 A resolution. A superposition of the structurally similar domains found in the heterodimer, alpha 1 onto alpha 2 and alpha 3 onto beta 2m, as well as the latter pair onto the ancestrally related immunoglobulin constant domain, reveals that differences are mainly in the turn regions. Structural features of the alpha 1 and alpha 2 domains, such as conserved salt-bridges that contribute to stability, specific loops that form contacts with other domains, and the antigen-binding groove formed from two adjacent helical regions on top of an eight-stranded beta-sheet, are analyzed. The interfaces between the domains, especially those between beta 2m and the HLA heavy chain presumably involved in beta 2m exchange and heterodimer assembly, are described in detail. A detailed examination of the binding groove confirms that the solvent-accessible amino acid side-chains that are most polymorphic in mouse and human alleles fill up the central and widest portion of the binding groove, while conserved side-chains are clustered at the narrower ends of the groove. Six pockets or sub-sites in the antigen-binding groove, of diverse shape and composition, appear suited for binding side-chains from antigenic peptides. Three pockets contain predominantly non-polar atoms; but others, especially those at the extreme ends of the groove, have clusters of polar atoms in close proximity to the "extra" electron density in the binding site. A possible role for beta 2m in stabilizing permissible peptide complexes during folding and assembly is presented.
+
The line below this paragraph, {{ABSTRACT_PUBMED_2038058}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 2038058 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_2038058}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Wiley, D C.]]
[[Category: Wiley, D C.]]
[[Category: Histocompatibility antigen]]
[[Category: Histocompatibility antigen]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:03:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 12:49:22 2008''

Revision as of 09:49, 3 July 2008

Image:3hla.png

Template:STRUCTURE 3hla

SPECIFICITY POCKETS FOR THE SIDE CHAINS OF PEPTIDE ANTIGENS IN HLA-AW68

Template:ABSTRACT PUBMED 2038058

About this Structure

3HLA is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution., Saper MA, Bjorkman PJ, Wiley DC, J Mol Biol. 1991 May 20;219(2):277-319. PMID:2038058

Page seeded by OCA on Thu Jul 3 12:49:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3hla"
Personal tools