1brv: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (13 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==SOLUTION NMR STRUCTURE OF THE IMMUNODOMINANT REGION OF PROTEIN G OF BOVINE RESPIRATORY SYNCYTIAL VIRUS, 48 STRUCTURES== | ||
<StructureSection load='1brv' size='340' side='right'caption='[[1brv]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1brv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovine_respiratory_syncytial_virus_(strain_391-2) Bovine respiratory syncytial virus (strain 391-2)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BRV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 48 models</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1brv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1brv OCA], [https://pdbe.org/1brv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1brv RCSB], [https://www.ebi.ac.uk/pdbsum/1brv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1brv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GLYC_BRSVC GLYC_BRSVC] Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection. Interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hemagglutinating activities (By similarity). Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors (By similarity). | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
== | Check<jmol> | ||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/1brv_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1brv ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The three-dimensional solution structure of the immunodominant central conserved region of the attachment protein G (BRSV-G) of bovine respiratory syncytial virus has been determined by nuclear magnetic resonance (NMR) spectroscopy. In the 32-residue peptide studied, 19 residues form a small rigid core composed of two short helices, connected by a type I' turn, and linked by two disulfide bridges. This unique fold is among the smallest stable tertiary structures known and could therefore serve as an ideal building block for the design of de novo proteins and as a test case for modeling studies. A characteristic hydrophobic pocket, lined by conserved residues, lies at the surface of the peptide and may play a role in receptor binding. This work provides a structural basis for further peptide vaccine development against the severe diseases associated with the respiratory syncytial viruses in both cattle and man. | The three-dimensional solution structure of the immunodominant central conserved region of the attachment protein G (BRSV-G) of bovine respiratory syncytial virus has been determined by nuclear magnetic resonance (NMR) spectroscopy. In the 32-residue peptide studied, 19 residues form a small rigid core composed of two short helices, connected by a type I' turn, and linked by two disulfide bridges. This unique fold is among the smallest stable tertiary structures known and could therefore serve as an ideal building block for the design of de novo proteins and as a test case for modeling studies. A characteristic hydrophobic pocket, lined by conserved residues, lies at the surface of the peptide and may play a role in receptor binding. This work provides a structural basis for further peptide vaccine development against the severe diseases associated with the respiratory syncytial viruses in both cattle and man. | ||
Solution structure of the immunodominant region of protein G of bovine respiratory syncytial virus.,Doreleijers JF, Langedijk JP, Hard K, Boelens R, Rullmann JA, Schaaper WM, van Oirschot JT, Kaptein R Biochemistry. 1996 Nov 26;35(47):14684-8. PMID:8942628<ref>PMID:8942628</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1brv" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
[[Category: Boelens | <references/> | ||
[[Category: Doreleijers | __TOC__ | ||
[[Category: Hard | </StructureSection> | ||
[[Category: Kaptein | [[Category: Large Structures]] | ||
[[Category: Langedijk | [[Category: Boelens R]] | ||
[[Category: Doreleijers JF]] | |||
[[Category: Rullmann | [[Category: Hard K]] | ||
[[Category: Schaaper | [[Category: Kaptein R]] | ||
[[Category: | [[Category: Langedijk JPM]] | ||
[[Category: Rullmann JAC]] | |||
[[Category: Schaaper WM]] | |||
[[Category: Van Oirschot JT]] | |||
Latest revision as of 11:21, 6 November 2024
SOLUTION NMR STRUCTURE OF THE IMMUNODOMINANT REGION OF PROTEIN G OF BOVINE RESPIRATORY SYNCYTIAL VIRUS, 48 STRUCTURESSOLUTION NMR STRUCTURE OF THE IMMUNODOMINANT REGION OF PROTEIN G OF BOVINE RESPIRATORY SYNCYTIAL VIRUS, 48 STRUCTURES
Structural highlights
FunctionGLYC_BRSVC Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection. Interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hemagglutinating activities (By similarity). Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe three-dimensional solution structure of the immunodominant central conserved region of the attachment protein G (BRSV-G) of bovine respiratory syncytial virus has been determined by nuclear magnetic resonance (NMR) spectroscopy. In the 32-residue peptide studied, 19 residues form a small rigid core composed of two short helices, connected by a type I' turn, and linked by two disulfide bridges. This unique fold is among the smallest stable tertiary structures known and could therefore serve as an ideal building block for the design of de novo proteins and as a test case for modeling studies. A characteristic hydrophobic pocket, lined by conserved residues, lies at the surface of the peptide and may play a role in receptor binding. This work provides a structural basis for further peptide vaccine development against the severe diseases associated with the respiratory syncytial viruses in both cattle and man. Solution structure of the immunodominant region of protein G of bovine respiratory syncytial virus.,Doreleijers JF, Langedijk JP, Hard K, Boelens R, Rullmann JA, Schaaper WM, van Oirschot JT, Kaptein R Biochemistry. 1996 Nov 26;35(47):14684-8. PMID:8942628[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||