2j9a

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(Difference between revisions)

@@ Line 6: / Line 6: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bll|1bll]], [[1bpm|1bpm]], [[1bpn|1bpn]], [[1lam|1lam]], [[1lan|1lan]], [[1lap|1lap]], [[1lcp|1lcp]], [[2ewb|2ewb]]</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=2j9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j9a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2j9a RCSB], [http://www.ebi.ac.uk/pdbsum/2j9a 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=2j9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j9a OCA], [http://pdbe.org/2j9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j9a RCSB], [http://www.ebi.ac.uk/pdbsum/2j9a PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2j9a" style="background-color:#fffaf0;"></div>
 ==See Also==

Revision as of 21:56, 9 September 2015

blLAP in Complex with Microginin FR1

spinqualitylabelsall models

2j9a, resolution 1.73Å

Show:Asymmetric Unit Biological Assembly

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Structural highlights

2j9a is a 2 chain structure with sequence from Bos taurus and Microcystis sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
NonStd Res:
Related:	1bll, 1bpm, 1bpn, 1lam, 1lan, 1lap, 1lcp, 2ewb
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[AMPL_BOVIN] Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.

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

Natural bioactive compounds are of general interest for pharmaceutical research because they may serve as leads in drug development campaigns. Among them, microginins are linear peptides known to inhibit various exopeptidases. The crystal structure of microginin FR1 from Microcystis sp. bound to bovine lens leucine aminopeptidase was established at 1.73 Angstrom resolution. The observed binding structure could be beneficial for the design of potent aminopeptidase inhibitors.

Binding structure of the leucine aminopeptidase inhibitor microginin FR1.,Kraft M, Schleberger C, Weckesser J, Schulz GE FEBS Lett. 2006 Dec 22;580(30):6943-7. Epub 2006 Dec 4. PMID:17157838^[1]

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

References

↑ Kraft M, Schleberger C, Weckesser J, Schulz GE. Binding structure of the leucine aminopeptidase inhibitor microginin FR1. FEBS Lett. 2006 Dec 22;580(30):6943-7. Epub 2006 Dec 4. PMID:17157838 doi:10.1016/j.febslet.2006.11.060

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

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2j9a

From Proteopedia

Revision as of 21:56, 9 September 2015

blLAP in Complex with Microginin FR1

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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