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1spj

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Revision as of 15:34, 27 October 2021

STRUCTURE OF MATURE HUMAN TISSUE KALLIKREIN (HUMAN KALLIKREIN 1 OR KLK1) AT 1.70 ANGSTROM RESOLUTION WITH VACANT ACTIVE SITE

Structural highlights

1spj is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	KLK1 (HUMAN)
Activity:	Tissue kallikrein, with EC number 3.4.21.35
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KLK1_HUMAN] Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Human kallikreins are serine proteases that comprise a recently identified large and closely related 15-member family. The kallikreins include both regulatory- and degradative-type proteases, impacting a variety of physiological processes including regulation of blood pressure, neuronal health, and the inflammatory response. While the function of the majority of the kallikreins remains to be elucidated, two members are useful biomarkers for prostate cancer and several others are potentially useful biomarkers for breast cancer, Alzheimer's, and Parkinson's disease. Human tissue kallikrein (human K1) is the best functionally characterized member of this family, and is known to play an important role in blood pressure regulation. As part of this function, human K1 exhibits unique dual-substrate specificity in hydrolyzing low molecular weight kininogen between both Arg-Ser and Met-Lys sequences. We report the X-ray crystal structure of mature, active recombinant human apo K1 at 1.70 A resolution. The active site exhibits structural features intermediate between that of apo and pro forms of known kallikrein structures. The S2 to S2' pockets demonstrate a variety of conformational changes in comparison to the porcine homolog of K1 in complex with peptide inhibitors, including the displacement of an extensive solvent network. These results indicate that the binding of a peptide substrate contributes to a structural rearrangement of the active-site Ser 195 resulting in a catalytically competent juxtaposition with the active-site His 57. The solvent networks within the S1 and S1' pockets suggest how the Arg-Ser and Met-Lys dual substrate specificity of human K1 is accommodated.

1.70 A X-ray structure of human apo kallikrein 1: structural changes upon peptide inhibitor/substrate binding.,Laxmikanthan G, Blaber SI, Bernett MJ, Scarisbrick IA, Juliano MA, Blaber M Proteins. 2005 Mar 1;58(4):802-14. PMID:15651049^[1]

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

References

↑ Laxmikanthan G, Blaber SI, Bernett MJ, Scarisbrick IA, Juliano MA, Blaber M. 1.70 A X-ray structure of human apo kallikrein 1: structural changes upon peptide inhibitor/substrate binding. Proteins. 2005 Mar 1;58(4):802-14. PMID:15651049 doi:10.1002/prot.20368

1 Structural highlights
2 Function
3 Evolutionary Conservation
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/1spj"

@@ Line 3: / Line 3: @@
 <StructureSection load='1spj' size='340' side='right'caption='[[1spj]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1spj]] is a 1 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=1SPJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SPJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1spj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SPJ FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KLK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KLK1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tissue_kallikrein Tissue kallikrein], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.35 3.4.21.35] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tissue_kallikrein Tissue kallikrein], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.35 3.4.21.35] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1spj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1spj OCA], [http://pdbe.org/1spj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1spj RCSB], [http://www.ebi.ac.uk/pdbsum/1spj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1spj ProSAT]</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=1spj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1spj OCA], [https://pdbe.org/1spj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1spj RCSB], [https://www.ebi.ac.uk/pdbsum/1spj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1spj ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KLK1_HUMAN KLK1_HUMAN]] Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
+[[https://www.uniprot.org/uniprot/KLK1_HUMAN KLK1_HUMAN]] Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1spj

From Proteopedia

Revision as of 15:34, 27 October 2021

STRUCTURE OF MATURE HUMAN TISSUE KALLIKREIN (HUMAN KALLIKREIN 1 OR KLK1) AT 1.70 ANGSTROM RESOLUTION WITH VACANT ACTIVE SITE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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