3kfq: Difference between revisions

Revision as of 18:39, 4 August 2016

Unreduced cathepsin V in complex with stefin AUnreduced cathepsin V in complex with stefin A

Structural highlights

3kfq is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1nb3, 1stf, 3k9m, 3a9n
Activity:	Cathepsin V, with EC number 3.4.22.43
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[CYTA_HUMAN] Defects in CSTA are the cause of ichthyosis exfoliative autosomal recessive ichthyosis bullosa of Siemens-like (AREI) [MIM:607936]. A form of congenital exfoliative ichthyosis, sharing some features with ichthyosis bullosa of Siemens and annular epidermolytic ichthyosis. AREI presents shortly after birth as dry, scaly skin over most of the body with coarse peeling of non-erythematous skin on the palms and soles, which is exacerbated by excessive moisture and minor trauma. Electron microscopy analysis of skin biopsies, reveals mostly normal-appearing upper layers of the epidermis, but prominent intercellular edema of the basal and suprabasal cell layers with aggregates of tonofilaments in the basal keratinocytes.^[1]

Function

[CATL2_HUMAN] Cysteine protease. May have an important role in corneal physiology.^[2] ^[3] [CYTA_HUMAN] This is an intracellular thiol proteinase inhibitor. Has an important role in desmosome-mediated cell-cell adhesion in the lower levels of the epidermis.^[4]

References

↑ Blaydon DC, Nitoiu D, Eckl KM, Cabral RM, Bland P, Hausser I, van Heel DA, Rajpopat S, Fischer J, Oji V, Zvulunov A, Traupe H, Hennies HC, Kelsell DP. Mutations in CSTA, encoding Cystatin A, underlie exfoliative ichthyosis and reveal a role for this protease inhibitor in cell-cell adhesion. Am J Hum Genet. 2011 Oct 7;89(4):564-71. doi: 10.1016/j.ajhg.2011.09.001. Epub, 2011 Sep 22. PMID:21944047 doi:10.1016/j.ajhg.2011.09.001
↑ Adachi W, Kawamoto S, Ohno I, Nishida K, Kinoshita S, Matsubara K, Okubo K. Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium. Invest Ophthalmol Vis Sci. 1998 Sep;39(10):1789-96. PMID:9727401
↑ Bromme D, Li Z, Barnes M, Mehler E. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry. 1999 Feb 23;38(8):2377-85. PMID:10029531 doi:10.1021/bi982175f
↑ Blaydon DC, Nitoiu D, Eckl KM, Cabral RM, Bland P, Hausser I, van Heel DA, Rajpopat S, Fischer J, Oji V, Zvulunov A, Traupe H, Hennies HC, Kelsell DP. Mutations in CSTA, encoding Cystatin A, underlie exfoliative ichthyosis and reveal a role for this protease inhibitor in cell-cell adhesion. Am J Hum Genet. 2011 Oct 7;89(4):564-71. doi: 10.1016/j.ajhg.2011.09.001. Epub, 2011 Sep 22. PMID:21944047 doi:10.1016/j.ajhg.2011.09.001

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OCA

[1] Blaydon DC, Nitoiu D, Eckl KM, Cabral RM, Bland P, Hausser I, van Heel DA, Rajpopat S, Fischer J, Oji V, Zvulunov A, Traupe H, Hennies HC, Kelsell DP. Mutations in CSTA, encoding Cystatin A, underlie exfoliative ichthyosis and reveal a role for this protease inhibitor in cell-cell adhesion. Am J Hum Genet. 2011 Oct 7;89(4):564-71. doi: 10.1016/j.ajhg.2011.09.001. Epub, 2011 Sep 22. PMID:21944047 doi:10.1016/j.ajhg.2011.09.001

[2] Adachi W, Kawamoto S, Ohno I, Nishida K, Kinoshita S, Matsubara K, Okubo K. Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium. Invest Ophthalmol Vis Sci. 1998 Sep;39(10):1789-96. PMID:9727401

[3] Bromme D, Li Z, Barnes M, Mehler E. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry. 1999 Feb 23;38(8):2377-85. PMID:10029531 doi:10.1021/bi982175f

[4] Blaydon DC, Nitoiu D, Eckl KM, Cabral RM, Bland P, Hausser I, van Heel DA, Rajpopat S, Fischer J, Oji V, Zvulunov A, Traupe H, Hennies HC, Kelsell DP. Mutations in CSTA, encoding Cystatin A, underlie exfoliative ichthyosis and reveal a role for this protease inhibitor in cell-cell adhesion. Am J Hum Genet. 2011 Oct 7;89(4):564-71. doi: 10.1016/j.ajhg.2011.09.001. Epub, 2011 Sep 22. PMID:21944047 doi:10.1016/j.ajhg.2011.09.001

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@@ Line 1: / Line 1: @@
 ==Unreduced cathepsin V in complex with stefin A==
 <StructureSection load='3kfq' size='340' side='right' caption='[[3kfq]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3kfq]] is a 4 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=3KFQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KFQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3kfq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KFQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KFQ FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nb3|1nb3]], [[1stf|1stf]], [[3k9m|3k9m]], [[3a9n|3a9n]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_V Cathepsin V], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.43 3.4.22.43] </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=3kfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kfq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kfq RCSB], [http://www.ebi.ac.uk/pdbsum/3kfq 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=3kfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kfq OCA], [http://pdbe.org/3kfq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kfq RCSB], [http://www.ebi.ac.uk/pdbsum/3kfq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kfq ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 20: / Line 21: @@
 </StructureSection>
 [[Category: Cathepsin V]]
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Renko, M]]
 [[Category: Turk, D]]

3kfq: Difference between revisions

Revision as of 18:39, 4 August 2016

Unreduced cathepsin V in complex with stefin AUnreduced cathepsin V in complex with stefin A

Structural highlights

Disease

Function

See Also

References

Contents

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3kfq: Difference between revisions

Revision as of 18:39, 4 August 2016

Unreduced cathepsin V in complex with stefin AUnreduced cathepsin V in complex with stefin A

Structural highlights

Disease

Function

See Also

References

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