1lds
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1lds.jpg|left|200px]] | [[Image:1lds.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1lds", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1lds| PDB=1lds | SCENE= }} | |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''Crystal Structure of monomeric human beta-2-microglobulin''' | '''Crystal Structure of monomeric human beta-2-microglobulin''' | ||
| Line 33: | Line 30: | ||
[[Category: Smith, D P.]] | [[Category: Smith, D P.]] | ||
[[Category: Trinh, C H.]] | [[Category: Trinh, C H.]] | ||
| - | [[Category: | + | [[Category: Immunoglobulin constant domain]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:49:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:49, 2 May 2008
Crystal Structure of monomeric human beta-2-microglobulin
Contents |
Overview
Dissociation of human beta-2-microglobulin (beta(2)m) from the heavy chain of the class I HLA complex is a critical first step in the formation of amyloid fibrils from this protein. As a consequence of renal failure, the concentration of circulating monomeric beta(2)m increases, ultimately leading to deposition of the protein into amyloid fibrils and development of the disorder, dialysis-related amyloidosis. Here we present the crystal structure of a monomeric form of human beta(2)m determined at 1.8-A resolution that reveals remarkable structural changes relative to the HLA-bound protein. These involve the restructuring of a beta bulge that separates two short beta strands to form a new six-residue beta strand at one edge of this beta sandwich protein. These structural changes remove key features proposed to have evolved to protect beta sheet proteins from aggregation [Richardson, J. & Richardson, D. (2002) Proc. Natl. Acad. Sci. USA 99, 2754-2759] and replaces them with an aggregation-competent surface. In combination with solution studies using (1)H NMR, we show that the crystal structure presented here represents a rare species in solution that could provide important clues about the mechanism of amyloid formation from the normally highly soluble native protein.
Disease
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]
About this Structure
1LDS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties., Trinh CH, Smith DP, Kalverda AP, Phillips SE, Radford SE, Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9771-6. Epub 2002 Jul 15. PMID:12119416 Page seeded by OCA on Fri May 2 23:49:41 2008
