3oe6

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==About this Structure==
==About this Structure==
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[[3oe6]] is a 1 chain structure of [[CXC chemokine receptor type 4]] and [[Hen Egg-White (HEW) Lysozyme]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens,_enterobacteria_phage_t4 Homo sapiens, enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OE6 OCA].
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[[3oe6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OE6 OCA].
==See Also==
==See Also==
*[[CXC chemokine receptor type 4|CXC chemokine receptor type 4]]
*[[CXC chemokine receptor type 4|CXC chemokine receptor type 4]]
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*[[G protein-coupled receptor|G protein-coupled receptor]]
*[[Hen Egg-White (HEW) Lysozyme|Hen Egg-White (HEW) Lysozyme]]
*[[Hen Egg-White (HEW) Lysozyme|Hen Egg-White (HEW) Lysozyme]]
==Reference==
==Reference==
<ref group="xtra">PMID:020929726</ref><references group="xtra"/>
<ref group="xtra">PMID:020929726</ref><references group="xtra"/>
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[[Category: Homo sapiens, enterobacteria phage t4]]
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[[Category: Homo sapiens]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: ATCG3D, Accelerated Technologies Center for Gene to 3D Structure.]]
[[Category: ATCG3D, Accelerated Technologies Center for Gene to 3D Structure.]]

Revision as of 10:42, 20 October 2012

Template:STRUCTURE 3oe6

Contents

Crystal structure of the CXCR4 chemokine receptor in complex with a small molecule antagonist IT1t in I222 spacegroup

Publication Abstract from PubMed

Chemokine receptors are critical regulators of cell migration in the context of immune surveillance, inflammation, and development. The G protein-coupled chemokine receptor, CXCR4, is specifically implicated in cancer metastasis and HIV-1 infection. Here, we report five independent crystal structures of CXCR4 bound to an antagonist small molecule IT1t and a cyclic peptide CVX15 at 2.5 to 3.2 angstrom resolution. All structures reveal a consistent homodimer with an interface including helices V and VI that may be involved in regulating signaling. The location and shape of the ligand-binding sites differ from other G protein-coupled receptors (GPCRs) and are closer to the extracellular surface. These structures provide new clues about the interactions between CXCR4 and its natural ligand CXCL12 and with the HIV-1 glycoprotein gp120.

Structures of the CXCR4 Chemokine GPCR with Small-Molecule and Cyclic Peptide Antagonists., Wu B, Chien EY, Mol CD, Fenalti G, Liu W, Katritch V, Abagyan R, Brooun A, Wells P, Bi FC, Hamel DJ, Kuhn P, Handel TM, Cherezov V, Stevens RC, Science. 2010 Oct 7. PMID:20929726

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3oe6 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Wu B, Chien EY, Mol CD, Fenalti G, Liu W, Katritch V, Abagyan R, Brooun A, Wells P, Bi FC, Hamel DJ, Kuhn P, Handel TM, Cherezov V, Stevens RC. Structures of the CXCR4 Chemokine GPCR with Small-Molecule and Cyclic Peptide Antagonists. Science. 2010 Oct 7. PMID:20929726 doi:10.1126/science.1194396

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