Proteins Binding to the Carbohydrate HNK-1: Common Origins?

Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067 (Electronic) Linking ISSN: 14220067 NLM ISO Abbreviation: Int J Mol Sci Subsets: MEDLINE

Original Publication: Basel, Switzerland : MDPI, [2000-

CD57 Antigens/*metabolism ; Cadherins/*metabolism ; HMGB1 Protein/*metabolism ; HMGB2 Protein/*metabolism ; Laminin/*metabolism ; Oligosaccharides/*metabolism; Amino Acid Sequence ; Animals ; Binding Sites ; CD57 Antigens/chemistry ; Cadherins/chemistry ; HMGB1 Protein/chemistry ; HMGB2 Protein/chemistry ; Humans ; Laminin/chemistry ; Ligands ; Nerve Regeneration/physiology ; Neuronal Plasticity/physiology ; Oligosaccharides/chemistry ; Protein Binding ; Protein Domains

The human natural killer (HNK-1) carbohydrate plays important roles during nervous system development, regeneration after trauma and synaptic plasticity. Four proteins have been identified as receptors for HNK-1: the laminin adhesion molecule, high-mobility group box 1 and 2 (also called amphoterin) and cadherin 2 (also called N-cadherin). Because of HNK-1's importance, we asked whether additional receptors for HNK-1 exist and whether the four identified proteins share any similarity in their primary structures. A set of 40,000 sequences homologous to the known HNK-1 receptors was selected and used for large-scale sequence alignments and motif searches. Although there are conserved regions and highly conserved sites within each of these protein families, there was no sequence similarity or conserved sequence motifs found to be shared by all families. Since HNK-1 receptors have not been compared regarding binding constants and since it is not known whether the sulfated or non-sulfated part of HKN-1 represents the structurally crucial ligand, the receptors are more heterogeneous in primary structure than anticipated, possibly involving different receptor or ligand regions. We thus conclude that the primary protein structure may not be the sole determinant for a bona fide HNK-1 receptor, rendering receptor structure more complex than originally assumed.

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Keywords: HNK-1; carbohydrate; development; receptor; sequence comparison

0 (CD57 Antigens)
0 (Cadherins)
0 (HMGB1 Protein)
0 (HMGB2 Protein)
0 (Laminin)
0 (Ligands)
0 (Oligosaccharides)
0 (laminin 1)

Date Created: 20210807 Date Completed: 20210914 Latest Revision: 20210914

20231215

PMC8347730

10.3390/ijms22158116

34360882