User:Kristian Koski/P4H

(Difference between revisions)

Revision as of 12:39, 28 February 2019

↑ Koski MK, Hieta R, Hirsila M, Ronka A, Myllyharju J, Wierenga RK. The crystal structure of an algal prolyl 4-hydroxylase complexed with a proline-rich peptide reveals a novel buried tripeptide binding motif. J Biol Chem. 2009 Sep 11;284(37):25290-301. Epub 2009 Jun 24. PMID:19553701 doi:10.1074/jbc.M109.014050

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 <StructureSection load='3gze' size='340' side='right' caption='Caption for this structure' scene=''>
-This is a default text for your page '''Kristian Koski/P4H'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
+Chlamydomonas reinhardtii prolyl 4-hydroxylase is a monomeric enzyme which catalyse the hydroxylation of proline residues of the proline-rich cell wall proteins. The structure of Cr-P4H has been determined as apo and in complexed with Zinc and serine-proline rich peptide<ref>pmid 19553701</ref>.
-You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
+== Function ==http://proteopedia.org/wiki/index.php?title=User:Kristian_Koski/P4H&action=edit
+Prolyl 4-hydroxylase (P4H) catalyses the hydroxylation of a proline resiue in the collagens .
-== Function ==
-Prolyl 4-hydroxylase (P4H) catalyses the hydroxylation of a proline resiue in the collagens <ref>pmid 19553701</ref>.
 == Disease ==