4pz3 | pdb_00004pz3

High-resolution crystal structure of the human CD44 hyaluronan binding domain complex with undefined peptides

spinqualitylabelsall models 4pz3, resolution 1.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pz3 is a 3 chain structure with sequence from Escherichia coli and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.083Å Ligands: EDO, MES, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CD44_HUMAN Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events. Publication Abstract from PubMed Two new crystal structures of the extracellular hyaluronan-binding domain of human CD44 are described at high resolution. A hexagonal crystal form at 1.60 A resolution and a monoclinic form at 1.08 A resolution both have two molecules in the asymmetric unit arranged about a similar noncrystallographic twofold axis of symmetry. These structures are compared with those previously reported at 2.20 A resolution to show that the fold is quite resistant to structural deformation in different crystal environments. Unexpectedly, a short peptide is found in the monoclinic crystals at a site remote from the known hyaluronan-binding groove. The peptide with a valine at the carboxy-terminus must have co-purified from the bacterial expression host and binds on the opposite side of the domain from the known hyaluronan-binding groove. This opportunistic binding may identify a site of interaction used as CD44 assembles with other proteins to accomplish effective signaling regarding changes to the extracellular environment. High-resolution crystal structures of alternate forms of the human CD44 hyaluronan-binding domain reveal a site for protein interaction.,Liu LK, Finzel B Acta Crystallogr F Struct Biol Commun. 2014 Sep 1;70(Pt 9):1155-61. doi:, 10.1107/S2053230X14015532. Epub 2014 Aug 29. PMID:25195884 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CD44

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