2zb6
From Proteopedia
(New page: 200px<br /><applet load="2zb6" size="350" color="white" frame="true" align="right" spinBox="true" caption="2zb6, resolution 2.60Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | Measles still remains a major cause of childhood morbidity and mortality | + | Measles still remains a major cause of childhood morbidity and mortality worldwide. Measles virus (MV) vaccines are highly successful, but the mechanism underlying their efficacy has been unclear. Here we report the crystal structure of the MV attachment protein, hemagglutinin, responsible for MV entry. The receptor-binding head domain exhibits a cubic-shaped beta-propeller structure and forms a homodimer. N-linked sugars appear to mask the broad regions and cause the two molecules forming the dimer to tilt oppositely toward the horizontal plane. Accordingly, residues of the putative receptor-binding site, highly conserved among MV strains, are strategically positioned in the unshielded area of the protein. These conserved residues also serve as epitopes for neutralizing antibodies, ensuring the serological monotype, a basis for effective MV vaccines. Our findings suggest that sugar moieties in the MV hemagglutinin critically modulate virus-receptor interaction as well as antiviral antibody responses, differently from sugars of the HIV gp120, which allow for immune evasion. |
==About this Structure== | ==About this Structure== | ||
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[[Category: virion]] | [[Category: virion]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:01:12 2008'' |
Revision as of 17:01, 21 February 2008
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Crystal structure of the measles virus hemagglutinin (oligo-sugar type)
Overview
Measles still remains a major cause of childhood morbidity and mortality worldwide. Measles virus (MV) vaccines are highly successful, but the mechanism underlying their efficacy has been unclear. Here we report the crystal structure of the MV attachment protein, hemagglutinin, responsible for MV entry. The receptor-binding head domain exhibits a cubic-shaped beta-propeller structure and forms a homodimer. N-linked sugars appear to mask the broad regions and cause the two molecules forming the dimer to tilt oppositely toward the horizontal plane. Accordingly, residues of the putative receptor-binding site, highly conserved among MV strains, are strategically positioned in the unshielded area of the protein. These conserved residues also serve as epitopes for neutralizing antibodies, ensuring the serological monotype, a basis for effective MV vaccines. Our findings suggest that sugar moieties in the MV hemagglutinin critically modulate virus-receptor interaction as well as antiviral antibody responses, differently from sugars of the HIV gp120, which allow for immune evasion.
About this Structure
2ZB6 is a Single protein structure of sequence from Measles virus with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of measles virus hemagglutinin provides insight into effective vaccines., Hashiguchi T, Kajikawa M, Maita N, Takeda M, Kuroki K, Sasaki K, Kohda D, Yanagi Y, Maenaka K, Proc Natl Acad Sci U S A. 2007 Dec 4;104(49):19535-40. Epub 2007 Nov 14. PMID:18003910
Page seeded by OCA on Thu Feb 21 19:01:12 2008
Categories: Measles virus | Single protein | Hashiguchi, T. | Kajikawa, M. | Kohda, D. | Kuroki, K. | Maenaka, K. | Maita, N. | Sasaki, K. | Takeda, M. | Yanagi, Y. | NAG | Beta propeller | Envelope protein | Hemagglutinin | Membrane | Transmembrane | Viral protein | Virion
