LH1 TYR511END
SiMPLOD ID   This is the unique identifier for this mutation in the SiMPLOD database. Please use this identifier when linking information described in SiMPLOD about this mutation.	SiMPLOD1-209
Isoenzyme   Follow the links to gather information about the LH1 isoenzyme	Lysyl Hydroxylase 1 (human) - UniProt - Full Info
Nucleotide mutation   Follow the links to explore annotated information about the significance of the PLOD1 c.1533C>G mutation	PLOD1 NM_000302.2:c.1533C>G - NCBI RefSeq NCBI SNP: rs121913552 NCBI ClinVar: 14370
Mutation type   Current information about the clinical implications of the mutation	Pathogenic
LOVD   Link to Leiden Open Variation Database (LOVD)	c.1533C>G
Disease Phenotype   Annotated information about disease phenotypes associated to this mutation	Ehlers-Danlos syndrome, cardiovascular phenotype Link1
Clinical Databases   Link to clinical databases, including OMIM (Online Mendelian Inheritance in Man), Orphanet, ICD-10 (International Statistical Classification of Diseases and Related Health Problems, rev. 10), MeSH (Medical Subject Headings)	OMIM: 225320 Orphanet: ORPHA:230851 ICD-10: Q79.6 MeSH: C536198
Evidence at protein level   Based on available structural and biochemical information, a statement about the existence of an LH enzyme variant bearing the described mutation is provided	Warning: this variant incorporates a premature truncation of the aminoacid sequence at residue 511, and may result in misfolding and/or complete absence of the enzyme. This variant is EXTREMELY UNLIKELY to be compatible with a folded LH enzyme. The representation shown in the structure viewer is therefore for mere display purposes and does not refer to an actual predicted existing protein product.
References   Publications (and associated links) describing the mutation	Walker et al., 1999 - DOI - PubMed Yeowell et al., 2000 - DOI - PubMed Yeowell et al., 1997 - PubMed Pousi et al., 2000 - DOI - PubMed
Notes from publications   A curated excerpt with information about the mutation from the publications found above	The C1557 to G point mutation produces a premature termination codon at Tyr511, in exon 14 of the PLOD1 gene. Several authors described this mutation to be present in skin fibroblast of at least five different unrelated patients with Ehlers-Danlos syndrome type VI. This mutation results in low levels of lysyl-hydroxylase activity measured in skin fibroblasts of the patients.
Structural Observations   An evaluation of the possible effects/implications of the mutations on the LH1 molecular structure
Related Entries   A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized	SiMPLOD1-134: LH1 dupl326-585;TYR455THRFS (Pathogenic) SiMPLOD1-325: LH1 delta491-550 (Pathogenic) SiMPLOD3-297: LH3 TYR521END (for biochemistry) SiMPLOD3-470: LH3 TYR521CYS (SNP) SiMPLOD3-524: LH3 TYR521TYR (SNP) SiMPLOD6-332: LH2b TYR542THRFS (Pathogenic)
Last Update   An evaluation of the possible effects/implications of the mutations on the LH1 molecular structure	2021-06-23 08:38:51
The three-dimensional visualization is currently based on the homology model of full-length, dimeric human LH1 (generated using the crystal structure of full-length human LH3 as template). You may select a different PDB model file to visualize the mutation(s) using the drop-down menu below (page will refresh): LH1 homology modelLH3 with Fe2+ and 2-OG (PDB 6FXK)