Sandbox GGC7: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

James Nolan, Student

@@ Line 6: / Line 6: @@
 Iduronate 2-sulfatase is located in the lysosome.[1] It is involved in the lysosomal degradation pathway of dermatan sulfate and heparan sulfate.[1] IDS hydrolyzes the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin.[1] Dermatan sulfate and heparan sulfate are complex glycosaminoglycans, which are essentially large sugar molecules.[2] They play important roles in cell adhesion, growth, proliferation and repair, and their degradation and recycling in the lysosome are essential for cellular maintenance.[2] IDS is expressed in the tissues of the liver, kidney, lung, and placenta.[1]
-== Relevance ==
+== Disease ==
-Mutations in Iduronate 2-sulfatase on the Xq28 chromosome can lead to Mucopolsaccharidosis 2 (MPS2), more commonly known as Hunter syndrome.[1] MPS2 is an X-linked lysosomal storage disease.[1] Due to the loss of IDS activity, the disease is characterized by the intracellular accumulation of the glycosaminoglycans heparan sulfate and dermatan sulfate, which are then excreted in urine.[1] Scientists have identified over 500 mutations on the Xq28 chromosome that include rearrangements, insertions/deletions, splicing defects and nonsense point mutations.[2] It is rare to find adults with Hunter syndrome as the average life expectancy for those with MPS2 is 15 years of age.[1] Most children diagnosed with MPS2 have somatic abnormalities including skeletal deformities, hepatosplenomegaly, and progressive cardiopulmonary deterioration.[1] Neurological damage is also prevalent beginning with what seems to be a developmental delay and hyperactivity, but progresses to mental retardation and dementia.[1] Death from MPS2 is typically due to obstructive airway disease or cardiac failure.[1]
+Mutations in Iduronate 2-sulfatase on the Xq28 chromosome can lead to Mucopolysaccharidosis 2 (MPS2), more commonly known as Hunter syndrome.[1] MPS2 is an X-linked lysosomal storage disease.[1] Due to the loss of IDS activity, the disease is characterized by the intracellular accumulation of the glycosaminoglycans heparan sulfate and dermatan sulfate, which are then excreted in urine.[1] Scientists have identified over 500 mutations on the Xq28 chromosome that include rearrangements, insertions/deletions, splicing defects and nonsense point mutations.[2] It is rare to find adults with severe Hunter syndrome as the average life expectancy for those with MPS2 is 15 years of age.[1] Most children diagnosed with MPS2 have somatic abnormalities including skeletal deformities, hepatosplenomegaly, and progressive cardiopulmonary deterioration.[1] Neurological damage is also prevalent beginning with what seems to be a developmental delay and hyperactivity, but progresses to mental retardation and dementia.[1] Death from MPS2 is typically due to obstructive airway disease or cardiac failure.[1] A treatment for patients with mild Hunter syndrome is enzyme replacement therapy, which involves the recombinant human IDS.[2]
 [[Image:Signs-and-symptoms-of-hunter-syndrome.jpg]]
 == Structural highlights ==
-<scene name='75/752270/Ide_mutations/2'>Scene 1: Mutation locations</scene>
+<scene name='75/752270/Ide_mutations/1'>Scene 1: Location of mutations</scene>
 <scene name='75/752270/Ide_atp_binding-active_sites/1'>Scene 2: ATP binding active sites</scene>
@@ Line 16: / Line 16: @@
 <scene name='75/752270/Ide_n_and_c_terminals/1'>Scene 3: N and C terminals</scene>
-<scene name='75/752270/Subunit_a_just_for_protein/1'>Scene 4: Subunit A</scene>
+<scene name='75/752270/Active_site_on_chain_a/1'>Scene 4: Active sites</scene>
-<scene name='75/752270/Ide_polar_section_of_active/1'>Text To Be Displayed</scene>
 </StructureSection>
 == References ==
-<references/>
+. UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. Iduronate 2-sulfatase https://www.uniprot.org/uniprot/P22304#pathology_and_biotech (accessed Apr 28,  2021).
+. Demydchuk M, Hill CH, Zhou A, Bunkóczi G, Stein PE, Marchesan D, Deane JE, Read RJ. Insights into Hunter syndrome from the structure of iduronate-2-sulfatase. Nat Commun. 2017 Jun 8;8:15786. doi: 10.1038/ncomms15786. PMID: 28593992; PMCID: PMC5472762.