4kga

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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bdg|2bdg]], [[2bdi|2bdi]], [[2bdh|2bdh]], [[4kel|4kel]], [[4k8y|4k8y]], [[4k1e|4k1e]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bdg|2bdg]], [[2bdi|2bdi]], [[2bdh|2bdh]], [[4kel|4kel]], [[4k8y|4k8y]], [[4k1e|4k1e]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KLK4 ([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">KLK4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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=4kga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kga OCA], [http://pdbe.org/4kga PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kga RCSB], [http://www.ebi.ac.uk/pdbsum/4kga PDBsum]</span></td></tr>
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<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=4kga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kga OCA], [http://pdbe.org/4kga PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kga RCSB], [http://www.ebi.ac.uk/pdbsum/4kga PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kga ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KLK4_HUMAN KLK4_HUMAN]] Involved in enamel formation.<ref>PMID:15235027</ref>
[[http://www.uniprot.org/uniprot/KLK4_HUMAN KLK4_HUMAN]] Involved in enamel formation.<ref>PMID:15235027</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The kallikrein-related peptidase (KLK) family of proteases is involved in many aspects of human health and disease. One member of this family, KLK4, has been implicated in cancer development and metastasis. Understanding mechanisms of inactivation are critical to developing selective KLK4 inhibitors. We have determined the X-ray crystal structures of KLK4 in complex with both sunflower trypsin inhibitor-1 (SFTI-1) and a rationally designed SFTI-1 derivative to atomic (~1 A) resolution, as well as with bound nickel. These structures offer a structural rationalization for the potency and selectivity of these inhibitors, and together with MD simulation and computational analysis, reveal a dynamic pathway between the metal binding exosite and the active site, providing key details of a previously proposed allosteric mode of inhibition. Collectively, this work provides insight into both direct and indirect mechanisms of inhibition for KLK4 that have broad implications for the enzymology of the serine protease superfamily, and may potentially be exploited for the design of therapeutic inhibitors.
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Direct and indirect mechanisms of KLK4 inhibition revealed by structure and dynamics.,Riley BT, Ilyichova O, Costa MG, Porebski BT, de Veer SJ, Swedberg JE, Kass I, Harris JM, Hoke DE, Buckle AM Sci Rep. 2016 Oct 21;6:35385. doi: 10.1038/srep35385. PMID:27767076<ref>PMID:27767076</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4kga" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==

Revision as of 11:15, 2 November 2016

Crystal structure of kallikrein-related peptidase 4

4kga, resolution 2.32Å

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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