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.

3frr

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 06:48, 1 November 2017

Structure of human IST1(NTD) - (residues 1-189)(P21)

Structural highlights

3frr 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.
Related:	3frs, 3frt, 3frv
Gene:	IST1, KIAA0174 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[IST1_HUMAN] Proposed to be involved in specific functions of the ESCRT machinery. Is required for efficient abscission during cytokinesis, but not for HIV-1 budding. The involvement in the MVB pathway is not established. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells.^[1] ^[2]

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

Endosomal sorting complexes required for transport-III (ESCRT-III) subunits cycle between two states: soluble monomers and higher-order assemblies that bind and remodel membranes during endosomal vesicle formation, midbody abscission and enveloped virus budding. Here we show that the N-terminal core domains of increased sodium tolerance-1 (IST1) and charged multivesicular body protein-3 (CHMP3) form equivalent four-helix bundles, revealing that IST1 is a previously unrecognized ESCRT-III family member. IST1 and its ESCRT-III binding partner, CHMP1B, both form higher-order helical structures in vitro, and IST1-CHMP1 interactions are required for abscission. The IST1 and CHMP3 structures also reveal that equivalent downstream alpha5 helices can fold back against the core domains. Mutations within the CHMP3 core-alpha5 interface stimulate the protein's in vitro assembly and HIV-inhibition activities, indicating that dissociation of the autoinhibitory alpha5 helix from the core activates ESCRT-III proteins for assembly at membranes.

Structural basis for ESCRT-III protein autoinhibition.,Bajorek M, Schubert HL, McCullough J, Langelier C, Eckert DM, Stubblefield WM, Uter NT, Myszka DG, Hill CP, Sundquist WI Nat Struct Mol Biol. 2009 Jul;16(7):754-62. Epub 2009 Jun 14. PMID:19525971^[3]

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

References

↑ Bajorek M, Morita E, Skalicky JJ, Morham SG, Babst M, Sundquist WI. Biochemical analyses of human IST1 and its function in cytokinesis. Mol Biol Cell. 2009 Mar;20(5):1360-73. doi: 10.1091/mbc.E08-05-0475. Epub 2009, Jan 7. PMID:19129479 doi:http://dx.doi.org/10.1091/mbc.E08-05-0475
↑ Agromayor M, Carlton JG, Phelan JP, Matthews DR, Carlin LM, Ameer-Beg S, Bowers K, Martin-Serrano J. Essential role of hIST1 in cytokinesis. Mol Biol Cell. 2009 Mar;20(5):1374-87. doi: 10.1091/mbc.E08-05-0474. Epub 2009, Jan 7. PMID:19129480 doi:http://dx.doi.org/10.1091/mbc.E08-05-0474
↑ Bajorek M, Schubert HL, McCullough J, Langelier C, Eckert DM, Stubblefield WM, Uter NT, Myszka DG, Hill CP, Sundquist WI. Structural basis for ESCRT-III protein autoinhibition. Nat Struct Mol Biol. 2009 Jul;16(7):754-62. Epub 2009 Jun 14. PMID:19525971 doi:10.1038/nsmb.1621

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/3frr"

@@ Line 1: / Line 1: @@
 ==Structure of human IST1(NTD) - (residues 1-189)(P21)==
 <StructureSection load='3frr' size='340' side='right' caption='[[3frr]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3frs|3frs]], [[3frt|3frt]], [[3frv|3frv]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IST1, KIAA0174 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3frr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3frr OCA], [http://pdbe.org/3frr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3frr RCSB], [http://www.ebi.ac.uk/pdbsum/3frr 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=3frr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3frr OCA], [http://pdbe.org/3frr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3frr RCSB], [http://www.ebi.ac.uk/pdbsum/3frr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3frr ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 37: / Line 38: @@
 [[Category: Schubert, H L]]
 [[Category: Sundquist, W I]]
+[[Category: Alternative splicing]]
 [[Category: Chmp]]
 [[Category: Escrt]]

3frr

From Proteopedia

Revision as of 06:48, 1 November 2017

Structure of human IST1(NTD) - (residues 1-189)(P21)

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