Sandbox Reserved 1096: Difference between revisions
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{{Sandbox_ESBS_2019}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_ESBS_2019}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
='''Human | ='''Human Peptidylarginine Deiminase Type 2''' = | ||
==General Description== | ==General Description== | ||
<Structure load='4N20' size='450' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='4N20' size='450' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
'''''Protein Arginine Deiminase type 2 ''''' also known as '''''PAD2''''', is a calcium-dependent [https://en.wikipedia.org/wiki/Enzyme enzyme] that catalyzes in humans the conversion of [https://en.wikipedia.org/wiki/Arginine Arginine] residues into [https://en.wikipedia.org/wiki/Citrulline Citrulline] in a [https://en.wikipedia.org/wiki/Post-translational_modification post-translational modification] referred to as [https://en.wikipedia.org/wiki/Citrullination Citrullination]. The structure of '''''PAD2 Apoenzyme''''' described here was elucidated at a calcium concentration of 0mM (Ca2+) with a resolution of 1.657 Å by [https://en.wikipedia.org/wiki/X-ray_crystallography x-ray diffraction cristallography]<ref name="PDB">[https://www.rcsb.org/structure/4N20</ref> . The biological assembly of PAD2 consists of a head-to-tail dimer with immunoglobin-like domains and a nucleophilic [https://en.wikipedia.org/wiki/Cysteine cysteine] residue responsible of catalytic activity in the active site <ref name="ART1">DOI:10.1021/cb500933j</ref>. | '''''Protein Arginine Deiminase type 2 ''''' also known as '''''PAD2''''', is a calcium-dependent [https://en.wikipedia.org/wiki/Enzyme enzyme] that catalyzes in humans the conversion of [https://en.wikipedia.org/wiki/Arginine Arginine] residues into [https://en.wikipedia.org/wiki/Citrulline Citrulline] in a [https://en.wikipedia.org/wiki/Post-translational_modification post-translational modification] referred to as [https://en.wikipedia.org/wiki/Citrullination Citrullination]. The structure of '''''PAD2 Apoenzyme''''' described here was elucidated at a calcium concentration of 0mM (Ca2+) with a resolution of 1.657 Å by [https://en.wikipedia.org/wiki/X-ray_crystallography x-ray diffraction cristallography]<ref name="PDB">[https://www.rcsb.org/structure/4N20</ref> . The biological assembly of PAD2 consists of a head-to-tail dimer with immunoglobin-like domains and a nucleophilic [https://en.wikipedia.org/wiki/Cysteine cysteine] residue responsible of catalytic activity in the active site <ref name="ART1">DOI:10.1021/cb500933j</ref>. In humans, five genes clustered in a single locus code for Arginine deiminases: ''PADI1,PADI2,PADI3,PADI4,PADI6''<ref name="ARTFr">DOI:10.1051/medsci/201127149</ref>. Expression of different isoforms of PAD seem to depend strongly on cell types and tissues even though PAD2 may be an ubiquist protein <ref name="ARTFr" />. Peptidyl Arginine Deiminase type 2 appears to have an essential role in the development of Breast Cancer, Multiple Sclerosis and other degenerative disorders thus making it a potential target for inhibitor design. | ||
==Structural Features== | ==Structural Features== | ||
==='''Primary, secondary and tertiary structure'''=== | ==='''Primary, secondary and tertiary structure'''=== | ||
