CD44: Difference between revisions

Revision as of 16:32, 19 October 2017

Function

CD44 is a glycoprotein involved in cell-cell interactions. CD44 is a receptor of hyaluronic acid (HA). CD44 undergoes post-translational modification. Its sialofucosylation changes it to a form which directs migration of stem cells to bone marrow.^[1]

(2jcq).^[2]

Relevance

CD44 is a potential drug target for treatment of malignant neoplasms. Anti-CD44 antibody treatment lowers hyperglycemia and chronic inflammatory diseases.

Human CD44 hyaluronan-binding domain complex with tetrapeptide (magenta), PEG, MES and ethylene glycol (PDB code 4pz3)

Drag the structure with the mouse to rotate

3D structures of CD443D structures of CD44

Updated on 19-October-2017

1uuh, 4pz4 – hCD44 hyaluronan-binding domain – human
1poz, 2i83 - hCD44 hyaluronan-binding domain – NMR
2jcp - mCD44 hyaluronan-binding domain – mouse
2jcq, 2jcr - mCD44 hyaluronan-binding domain + 8-mer HA
4mrd, 4mre, 4mrf, 4mrg, 4mrh, 4np2, 4bzc, 4bzk - mCD44 hyaluronan-binding domain + inhibitor
5bzt, 5bzs, 5bzr, 5bzq, 5bzp, 5bzo, 5bzn, 5bzm, 5bzl, 5bzj, 5bzi, 5bzh, 5bzg, 5bzf, 5bze - mCD44 hyaluronan-binding domain (mutant) + inhibitor
4np3 - mCD44 hyaluronan-binding domain + tetrapeptide
4pz3 - hCD44 hyaluronan-binding domain + tetrapeptide

ReferencesReferences

↑ Liu LK, Finzel B. High-resolution crystal structures of alternate forms of the human CD44 hyaluronan-binding domain reveal a site for protein interaction. Acta Crystallogr F Struct Biol Commun. 2014 Sep 1;70(Pt 9):1155-61. doi:, 10.1107/S2053230X14015532. Epub 2014 Aug 29. PMID:25195884 doi:http://dx.doi.org/10.1107/S2053230X14015532
↑ Banerji S, Wright AJ, Noble M, Mahoney DJ, Campbell ID, Day AJ, Jackson DG. Structures of the Cd44-hyaluronan complex provide insight into a fundamental carbohydrate-protein interaction. Nat Struct Mol Biol. 2007 Mar;14(3):234-9. Epub 2007 Feb 11. PMID:17293874 doi:10.1038/nsmb1201

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Michal Harel, Alexander Berchansky, Joel L. Sussman

[1] Liu LK, Finzel B. High-resolution crystal structures of alternate forms of the human CD44 hyaluronan-binding domain reveal a site for protein interaction. Acta Crystallogr F Struct Biol Commun. 2014 Sep 1;70(Pt 9):1155-61. doi:, 10.1107/S2053230X14015532. Epub 2014 Aug 29. PMID:25195884 doi:http://dx.doi.org/10.1107/S2053230X14015532

[2] Banerji S, Wright AJ, Noble M, Mahoney DJ, Campbell ID, Day AJ, Jackson DG. Structures of the Cd44-hyaluronan complex provide insight into a fundamental carbohydrate-protein interaction. Nat Struct Mol Biol. 2007 Mar;14(3):234-9. Epub 2007 Feb 11. PMID:17293874 doi:10.1038/nsmb1201

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	<StructureSection load='4pz3' size='350' side='right' scene='' caption='Human CD44 hyaluronan-binding domain complex with tetrapeptide (PDB code [[4pz3]])'>		<StructureSection load='4pz3' size='350' side='right' scene='' caption='Human CD44 hyaluronan-binding domain complex with tetrapeptide (magenta), PEG, MES and ethylene glycol (PDB code [[4pz3]])'>