SiMPLOD v. 0.6.2 alpha

LH2a LEU714ASP (LH2a) - LEU735ASP (LH2b)

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.
SiMPLOD2-335

Isoenzyme
  Follow the links to gather information about the LH2a isoenzyme
Lysyl Hydroxylase 2a (human) - UniProt - Full Info

Mutation type
  Current information about the clinical implications of the mutation
Mutation for Biochemical Studies (not necessarily related to observed polymorphisms)

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
This variant EXISTS at the protein level: published experimental data support its existence as protein product.

LH Activity
  When available, biochemical data describing the lysyl hydroxylase activity of the mutant are reported
No experimental data available

References
  Publications (and associated links) describing the mutation
Guo et al., 2018 - DOI - PubMed

Notes from publications
  A curated excerpt with information about the mutation from the publications found above
To determine key residues in activity and dimerization Guo et al. performed site-directed mutagenesis on L230, a viral homolog of PLODs, and on PLOD2. The Leu714Asp mutation in PLOD2 disrupted the dimer. The same occurs in mimivirus L230. The corresponding mutation in PLOD3 is not sufficient to disrupt dimer as demonstrated by Scietti et al.

Structural Observations
  An evaluation of the possible effects/implications of the mutations on the LH2a molecular structure
This residue is at the LH2 dimer interface.

Related Entries
  A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized
SiMPLOD3-287: LH3 LEU715ASP (for biochemistry)
SiMPLOD3-288: LH3 LEU715ARG (for biochemistry)

Last Update
  An evaluation of the possible effects/implications of the mutations on the LH2a molecular structure
2021-06-23 08:38:51

The three-dimensional visualization is currently based on the homology model of full-length, dimeric human LH2a (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):

LH2a LEU714ASP (LH2a) - LEU735ASP (LH2b)
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.	SiMPLOD2-335
Isoenzyme Follow the links to gather information about the LH2a isoenzyme	Lysyl Hydroxylase 2a (human) - UniProt - Full Info
Mutation type Current information about the clinical implications of the mutation	Mutation for Biochemical Studies (not necessarily related to observed polymorphisms)
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	This variant EXISTS at the protein level: published experimental data support its existence as protein product.
LH Activity When available, biochemical data describing the lysyl hydroxylase activity of the mutant are reported	No experimental data available
References Publications (and associated links) describing the mutation	Guo et al., 2018 - DOI - PubMed
Notes from publications A curated excerpt with information about the mutation from the publications found above	To determine key residues in activity and dimerization Guo et al. performed site-directed mutagenesis on L230, a viral homolog of PLODs, and on PLOD2. The Leu714Asp mutation in PLOD2 disrupted the dimer. The same occurs in mimivirus L230. The corresponding mutation in PLOD3 is not sufficient to disrupt dimer as demonstrated by Scietti et al.
Structural Observations An evaluation of the possible effects/implications of the mutations on the LH2a molecular structure	This residue is at the LH2 dimer interface.
Related Entries A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized	SiMPLOD3-287: LH3 LEU715ASP (for biochemistry) SiMPLOD3-288: LH3 LEU715ARG (for biochemistry)
Last Update An evaluation of the possible effects/implications of the mutations on the LH2a molecular structure	2021-06-23 08:38:51
The three-dimensional visualization is currently based on the homology model of full-length, dimeric human LH2a (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):