1iv5: Difference between revisions
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< | ==New Crystal Form of Human CD81 Large Extracellular Loop.== | ||
<StructureSection load='1iv5' size='340' side='right'caption='[[1iv5]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1iv5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IV5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IV5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</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=1iv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iv5 OCA], [https://pdbe.org/1iv5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iv5 RCSB], [https://www.ebi.ac.uk/pdbsum/1iv5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iv5 ProSAT]</span></td></tr> | ||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/CD81_HUMAN CD81_HUMAN] Defects in CD81 are the cause of immunodeficiency common variable type 6 (CVID6) [MIM:[https://omim.org/entry/613496 613496]; also called antibody deficiency due to CD81 defect. CVID6 is a primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low.<ref>PMID:20237408</ref> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CD81_HUMAN CD81_HUMAN] May play an important role in the regulation of lymphoma cell growth. Interacts with a 16-kDa Leu-13 protein to form a complex possibly involved in signal transduction. May act as the viral receptor for HCV. | |||
== 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/iv/1iv5_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=1iv5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The large extracellular loop of human CD81, a tetraspanin mediating hepatitis C virus envelope protein E2 binding to human cells, has been crystallized in a hexagonal form. The three-dimensional structure, solved and refined at 2.6 A resolution (R-factor = 22.8%), shows that the protein adopts a dimeric assembly, based on an association interface built up by tetraspanin-conserved residues. Structural comparisons with the tertiary structure of human CD81 large extracellular loop, previously determined in a different crystal form, show marked conformational fluctuations in the molecular regions thought to be involved in binding to the viral protein, suggesting rules for recognition and assembly within the tetraspan web. | |||
Subunit association and conformational flexibility in the head subdomain of human CD81 large extracellular loop.,Kitadokoro K, Ponassi M, Galli G, Petracca R, Falugi F, Grandi G, Bolognesi M Biol Chem. 2002 Sep;383(9):1447-52. PMID:12437138<ref>PMID:12437138</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1iv5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[CD81|CD81]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Bolognesi | [[Category: Large Structures]] | ||
[[Category: Fabiana | [[Category: Bolognesi M]] | ||
[[Category: Galli | [[Category: Fabiana F]] | ||
[[Category: Grandi | [[Category: Galli G]] | ||
[[Category: Kitadokoro | [[Category: Grandi G]] | ||
[[Category: Marco | [[Category: Kitadokoro K]] | ||
[[Category: Petracca | [[Category: Marco P]] | ||
[[Category: Petracca R]] | |||
Latest revision as of 07:37, 17 October 2024
New Crystal Form of Human CD81 Large Extracellular Loop.New Crystal Form of Human CD81 Large Extracellular Loop.
Structural highlights
DiseaseCD81_HUMAN Defects in CD81 are the cause of immunodeficiency common variable type 6 (CVID6) [MIM:613496; also called antibody deficiency due to CD81 defect. CVID6 is a primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low.[1] FunctionCD81_HUMAN May play an important role in the regulation of lymphoma cell growth. Interacts with a 16-kDa Leu-13 protein to form a complex possibly involved in signal transduction. May act as the viral receptor for HCV. 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 large extracellular loop of human CD81, a tetraspanin mediating hepatitis C virus envelope protein E2 binding to human cells, has been crystallized in a hexagonal form. The three-dimensional structure, solved and refined at 2.6 A resolution (R-factor = 22.8%), shows that the protein adopts a dimeric assembly, based on an association interface built up by tetraspanin-conserved residues. Structural comparisons with the tertiary structure of human CD81 large extracellular loop, previously determined in a different crystal form, show marked conformational fluctuations in the molecular regions thought to be involved in binding to the viral protein, suggesting rules for recognition and assembly within the tetraspan web. Subunit association and conformational flexibility in the head subdomain of human CD81 large extracellular loop.,Kitadokoro K, Ponassi M, Galli G, Petracca R, Falugi F, Grandi G, Bolognesi M Biol Chem. 2002 Sep;383(9):1447-52. PMID:12437138[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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