1hum: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 1: Line 1:


==SOLUTION STRUCTURE OF THE CHEMOKINE HMIP-1BETA(SLASH)ACT-2 BY MULTI-DIMENSIONAL NMR: A NOVEL CHEMOKINE DIMER==
==SOLUTION STRUCTURE OF THE CHEMOKINE HMIP-1BETA(SLASH)ACT-2 BY MULTI-DIMENSIONAL NMR: A NOVEL CHEMOKINE DIMER==
<StructureSection load='1hum' size='340' side='right'caption='[[1hum]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1hum' size='340' side='right'caption='[[1hum]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1hum]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HUM FirstGlance]. <br>
<table><tr><td colspan='2'>[[1hum]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HUM FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hun|1hun]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1hum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hum OCA], [https://pdbe.org/1hum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hum RCSB], [https://www.ebi.ac.uk/pdbsum/1hum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hum ProSAT]</span></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=1hum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hum OCA], [https://pdbe.org/1hum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hum RCSB], [https://www.ebi.ac.uk/pdbsum/1hum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hum ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CCL4_HUMAN CCL4_HUMAN]] Monokine with inflammatory and chemokinetic properties. Binds to CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-beta induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form MIP-1-beta(3-69) retains the abilities to induce down-modulation of surface expression of the chemokine receptor CCR5 and to inhibit the CCR5-mediated entry of HIV-1 in T-cells. MIP-1-beta(3-69) is also a ligand for CCR1 and CCR2 isoform B.<ref>PMID:8525373</ref> <ref>PMID:10540332</ref> <ref>PMID:12070155</ref>
[https://www.uniprot.org/uniprot/CCL4_HUMAN CCL4_HUMAN] Monokine with inflammatory and chemokinetic properties. Binds to CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-beta induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form MIP-1-beta(3-69) retains the abilities to induce down-modulation of surface expression of the chemokine receptor CCR5 and to inhibit the CCR5-mediated entry of HIV-1 in T-cells. MIP-1-beta(3-69) is also a ligand for CCR1 and CCR2 isoform B.<ref>PMID:8525373</ref> <ref>PMID:10540332</ref> <ref>PMID:12070155</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 19: Line 19:
</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=1hum ConSurf].
</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=1hum ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional heteronuclear magnetic resonance spectroscopy. Human MIP-1 beta is a symmetric homodimer with a relative molecular mass of approximately 16 kilodaltons. The structure of the hMIP-1 beta monomer is similar to that of the related alpha chemokine interleukin-8 (IL-8). However, the quaternary structures of the two proteins are entirely distinct, and the dimer interface is formed by a completely different set of residues. Whereas the IL-8 dimer is globular, the hMIP-1 beta dimer is elongated and cylindrical. This provides a rational explanation for the absence of cross-binding and reactivity between the alpha and beta chemokine subfamilies. Calculation of the solvation free energies of dimerization suggests that the formation and stabilization of the two different types of dimers arise from the burial of hydrophobic residues.
High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.,Lodi PJ, Garrett DS, Kuszewski J, Tsang ML, Weatherbee JA, Leonard WJ, Gronenborn AM, Clore GM Science. 1994 Mar 25;263(5154):1762-7. PMID:8134838<ref>PMID:8134838</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1hum" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Clore, G M]]
[[Category: Clore GM]]
[[Category: Garrett, D S]]
[[Category: Garrett DS]]
[[Category: Gronenborn, A M]]
[[Category: Gronenborn AM]]
[[Category: Lodi, P J]]
[[Category: Lodi PJ]]

Revision as of 14:35, 27 March 2024

SOLUTION STRUCTURE OF THE CHEMOKINE HMIP-1BETA(SLASH)ACT-2 BY MULTI-DIMENSIONAL NMR: A NOVEL CHEMOKINE DIMERSOLUTION STRUCTURE OF THE CHEMOKINE HMIP-1BETA(SLASH)ACT-2 BY MULTI-DIMENSIONAL NMR: A NOVEL CHEMOKINE DIMER

Structural highlights

1hum is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCL4_HUMAN Monokine with inflammatory and chemokinetic properties. Binds to CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-beta induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form MIP-1-beta(3-69) retains the abilities to induce down-modulation of surface expression of the chemokine receptor CCR5 and to inhibit the CCR5-mediated entry of HIV-1 in T-cells. MIP-1-beta(3-69) is also a ligand for CCR1 and CCR2 isoform B.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Cocchi F, DeVico AL, Garzino-Demo A, Arya SK, Gallo RC, Lusso P. Identification of RANTES, MIP-1 alpha, and MIP-1 beta as the major HIV-suppressive factors produced by CD8+ T cells. Science. 1995 Dec 15;270(5243):1811-5. PMID:8525373
  2. ↑ Garlisi CG, Xiao H, Tian F, Hedrick JA, Billah MM, Egan RW, Umland SP. The assignment of chemokine-chemokine receptor pairs: TARC and MIP-1 beta are not ligands for human CC-chemokine receptor 8. Eur J Immunol. 1999 Oct;29(10):3210-5. PMID:10540332 doi:http://dx.doi.org/10.1002/(SICI)1521-4141(199910)29:10<3210::AID-IMMU3210>3.0.CO;2-W
  3. ↑ Guan E, Wang J, Roderiquez G, Norcross MA. Natural truncation of the chemokine MIP-1 beta /CCL4 affects receptor specificity but not anti-HIV-1 activity. J Biol Chem. 2002 Aug 30;277(35):32348-52. Epub 2002 Jun 17. PMID:12070155 doi:http://dx.doi.org/10.1074/jbc.M203077200
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1hum&oldid=4115572"