4PZ4

High-resolution crystal structure of the human CD44 hyaluronan binding domain in new space group

Summary for 4PZ4

• Entry DOI: 10.2210/pdb4pz4/pdb
• Related: 1UUH 4PZ3
• Descriptor: CD44 antigen, SULFATE ION, DI(HYDROXYETHYL)ETHER, ... (7 entities in total)
• Functional Keywords: link module, binding protein, hyaluronan, ectodomain, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Single-pass type I membrane protein: P16070
• Total number of polymer chains: 2
• Total formula weight: 35513.44

Authors

Liu, L.K.,Finzel, B. (deposition date: 2014-03-28, release date: 2014-09-17, Last modification date: 2024-11-06)

Primary citation

Liu, 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

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)