This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1ss6

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 13:55, 18 December 2019

Solution structure of SEP domain from human p47

Structural highlights

1ss6 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NSF1C_HUMAN] Reduces the ATPase activity of VCP. Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (By similarity). Inhibits the activity of CTSL (in vitro).

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

The solution structure of the human p47 SEP domain in a construct comprising residues G1-S2-p47(171-270) was determined by NMR spectroscopy. A structure-derived hypothesis about the domains' function was formulated and pursued in binding experiments with cysteine proteases. The SEP domain was found to be a reversible competitive inhibitor of cathepsin L with a Ki of 1.5 microM. The binding of G1-S2-p47(171-270) to cathepsin L was mapped by biochemical assays and the binding interface was investigated by NMR chemical shift perturbation experiments.

The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L.,Soukenik M, Diehl A, Leidert M, Sievert V, Bussow K, Leitner D, Labudde D, Ball LJ, Lechner A, Nagler DK, Oschkinat H FEBS Lett. 2004 Oct 22;576(3):358-62. PMID:15498563^[1]

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

References

↑ Soukenik M, Diehl A, Leidert M, Sievert V, Bussow K, Leitner D, Labudde D, Ball LJ, Lechner A, Nagler DK, Oschkinat H. The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L. FEBS Lett. 2004 Oct 22;576(3):358-62. PMID:15498563 doi:10.1016/j.febslet.2004.09.037

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ss6"

@@ Line 1: / Line 1: @@
 ==Solution structure of SEP domain from human p47==
-<StructureSection load='1ss6' size='340' side='right' caption='[[1ss6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1ss6' size='340' side='right'caption='[[1ss6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1ss6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SS6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SS6 FirstGlance]. <br>
@@ Line 32: / Line 32: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Ball, L J]]
 [[Category: Buessow, K]]

1ss6

From Proteopedia

Revision as of 13:55, 18 December 2019

Solution structure of SEP domain from human p47

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox