2dp4
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2dp4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium album] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DP4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DP4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2dp4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium album] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DP4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DP4 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3prk|3prk]], [[1bjr|1bjr]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3prk|3prk]], [[1bjr|1bjr]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dp4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2dp4 RCSB], [http://www.ebi.ac.uk/pdbsum/2dp4 PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dp4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2dp4 RCSB], [http://www.ebi.ac.uk/pdbsum/2dp4 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PRTK_TRIAL PRTK_TRIAL]] Hydrolyzes keratin at aromatic and hydrophobic residues. [[http://www.uniprot.org/uniprot/TRFL_HUMAN TRFL_HUMAN]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref> Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref> Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref> The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref> Isoform DeltaLf: transcription factor with antiproliferative properties and inducing cell cycle arrest. Binds to DeltaLf response element found in the SKP1, BAX, DCPS, and SELH promoters.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Proteinase|Proteinase]] | *[[Proteinase|Proteinase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Peptidase K]] | [[Category: Peptidase K]] | ||
| - | [[Category: Bhushan, A | + | [[Category: Bhushan, A]] |
| - | [[Category: Sharma, S | + | [[Category: Sharma, S]] |
| - | [[Category: Singh, A K | + | [[Category: Singh, A K]] |
| - | [[Category: Singh, N | + | [[Category: Singh, N]] |
| - | [[Category: Singh, T P | + | [[Category: Singh, T P]] |
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Lactoferrin fragment]] | [[Category: Lactoferrin fragment]] | ||
[[Category: Proteinase k]] | [[Category: Proteinase k]] | ||
Revision as of 00:50, 25 December 2014
Crystal structure of the complex formed between proteinase K and a human lactoferrin fragment at 2.9 A resolution
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