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3ncl

From Proteopedia

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Current revision

Crystal Structure of MT-SP1 bound to Benzamidine Phosphonate Inhibitor

Structural highlights

3ncl is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.19Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ST14_HUMAN Defects in ST14 are a cause of ichthyosis autosomal recessive with hypotrichosis (ARIH) [MIM:610765. ARIH is a skin disorder characterized by congenital ichthyosis associated with the presence of less than the normal amount of hair.^[1]

Function

ST14_HUMAN Degrades extracellular matrix. Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site.

Publication Abstract from PubMed

The ability to follow enzyme activity in a cellular context represents a challenging technological frontier that impacts fields ranging from disease pathogenesis to epigenetics. Activity-based probes (ABPs) label the active form of an enzyme via covalent modification of catalytic residues. Here we present an analysis of parameters influencing potency of peptide phosphonate ABPs for trypsin-fold S1A proteases, an abundant and important class of enzymes with similar substrate specificities. We find that peptide length and stability influence potency more than sequence composition and present structural evidence that steric interactions at the prime-side of the substrate-binding cleft affect potency in a protease-dependent manner. We introduce guidelines for the design of peptide phosphonate ABPs and demonstrate their utility in a live-cell labeling application that specifically targets active S1A proteases at the cell surface of cancer cells.

Peptide length and leaving-group sterics influence potency of Peptide phosphonate protease inhibitors.,Brown CM, Ray M, Eroy-Reveles AA, Egea P, Tajon C, Craik CS Chem Biol. 2011 Jan 28;18(1):48-57. PMID:21276938^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Basel-Vanagaite L, Attia R, Ishida-Yamamoto A, Rainshtein L, Ben Amitai D, Lurie R, Pasmanik-Chor M, Indelman M, Zvulunov A, Saban S, Magal N, Sprecher E, Shohat M. Autosomal recessive ichthyosis with hypotrichosis caused by a mutation in ST14, encoding type II transmembrane serine protease matriptase. Am J Hum Genet. 2007 Mar;80(3):467-77. Epub 2007 Jan 23. PMID:17273967 doi:S0002-9297(07)60095-0
↑ Brown CM, Ray M, Eroy-Reveles AA, Egea P, Tajon C, Craik CS. Peptide length and leaving-group sterics influence potency of Peptide phosphonate protease inhibitors. Chem Biol. 2011 Jan 28;18(1):48-57. PMID:21276938 doi:10.1016/j.chembiol.2010.11.007

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ncl"

Categories: Homo sapiens | Large Structures | Brown C | Egea P | Ray M

@@ Line 1: / Line 1: @@
 ==Crystal Structure of MT-SP1 bound to Benzamidine Phosphonate Inhibitor==
-<StructureSection load='3ncl' size='340' side='right' caption='[[3ncl]], [[Resolution|resolution]] 1.19&Aring;' scene=''>
+<StructureSection load='3ncl' size='340' side='right'caption='[[3ncl]], [[Resolution|resolution]] 1.19&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ncl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NCL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NCL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ncl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NCL FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCZ:PHENYL+(4-CARBAMIMIDOYLBENZYL)PHOSPHONATE'>CCZ</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.19&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ST14, PRSS14, SNC19, TADG15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CCZ:PHENYL+(4-CARBAMIMIDOYLBENZYL)PHOSPHONATE'>CCZ</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Matriptase Matriptase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.109 3.4.21.109] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ncl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ncl OCA], [https://pdbe.org/3ncl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ncl RCSB], [https://www.ebi.ac.uk/pdbsum/3ncl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ncl ProSAT]</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=3ncl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ncl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ncl RCSB], [http://www.ebi.ac.uk/pdbsum/3ncl PDBsum]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/ST14_HUMAN ST14_HUMAN]] Defects in ST14 are a cause of ichthyosis autosomal recessive with hypotrichosis (ARIH) [MIM:[http://omim.org/entry/610765 610765]]. ARIH is a skin disorder characterized by congenital ichthyosis associated with the presence of less than the normal amount of hair.<ref>PMID:17273967</ref>
+[https://www.uniprot.org/uniprot/ST14_HUMAN ST14_HUMAN] Defects in ST14 are a cause of ichthyosis autosomal recessive with hypotrichosis (ARIH) [MIM:[https://omim.org/entry/610765 610765]. ARIH is a skin disorder characterized by congenital ichthyosis associated with the presence of less than the normal amount of hair.<ref>PMID:17273967</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/ST14_HUMAN ST14_HUMAN]] Degrades extracellular matrix. Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site.
+[https://www.uniprot.org/uniprot/ST14_HUMAN ST14_HUMAN] Degrades extracellular matrix. Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3ncl" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Matriptase|Matriptase]]
+*[[Matriptase 3D structures|Matriptase 3D structures]]
 == References ==
 <references/>
@@ Line 28: / Line 29: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Matriptase]]
+[[Category: Large Structures]]
-[[Category: Brown, C]]
+[[Category: Brown C]]
-[[Category: Egea, P]]
+[[Category: Egea P]]
-[[Category: Ray, M]]
+[[Category: Ray M]]
-[[Category: Benzamidine]]
-[[Category: Hydrolase]]
-[[Category: Phosphonate]]
-[[Category: Proteinase-inhibitor complex]]
-[[Category: Serine endopeptidase]]
-[[Category: Serine proteinase]]

3ncl

From Proteopedia

Current revision

Crystal Structure of MT-SP1 bound to Benzamidine Phosphonate Inhibitor

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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