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4PZ3

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

Summary for 4PZ3
Entry DOI10.2210/pdb4pz3/pdb
Related1UUH 4PZ4
DescriptorCD44 antigen, Undefined peptides modeled as AAAV, DI(HYDROXYETHYL)ETHER, ... (6 entities in total)
Functional Keywordslink module, binding protein, hyaluronan, ectodomain, cell adhesion
Biological sourceHomo sapiens (human)
More
Cellular locationCell membrane; Single-pass type I membrane protein: P16070
Total number of polymer chains3
Total formula weight34675.80
Authors
Liu, L.K.,Finzel, B. (deposition date: 2014-03-28, release date: 2014-09-17, Last modification date: 2024-10-16)
Primary citationLiu, L.K.,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, 70:1155-1161, 2014
Cited by
PubMed Abstract: 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 Å resolution and a monoclinic form at 1.08 Å 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 Å 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.
PubMed: 25195884
DOI: 10.1107/S2053230X14015532
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.083 Å)
Structure validation

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