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7df7

From Proteopedia

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Current revision

Crystal structure of human V-1 in the apo form

Structural highlights

7df7 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MTPN_HUMAN Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity (By similarity). Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy.^[1] ^[2] ^[3]

Publication Abstract from PubMed

V-1, also known as myotrophin, is a 13 kDa ankyrin-repeat protein that binds and inhibits the heterodimeric actin capping protein (CP), which is a key regulator of cytoskeletal actin dynamics. The crystal structure of V-1 in complex with CP revealed that V-1 recognizes CP via residues spanning several ankyrin repeats. Here, the crystal structure of human V-1 is reported in the absence of the specific ligand at 2.3 A resolution. In the asymmetric unit, the crystal contains two V-1 monomers that exhibit nearly identical structures (C(alpha) r.m.s.d. of 0.47 A). The overall structures of the two apo V-1 chains are also highly similar to that of CP-bound V-1 (C(alpha) r.m.s.d.s of <0.50 A), indicating that CP does not induce a large conformational change in V-1. Detailed structural comparisons using the computational program All Atom Motion Tree revealed that CP binding can be accomplished by minor side-chain rearrangements of several residues. These findings are consistent with the known biological role of V-1, in which it globally inhibits CP in the cytoplasm.

Crystal structure of human V-1 in the apo form.,Takeda S, Koike R, Nagae T, Fujiwara I, Narita A, Maeda Y, Ota M Acta Crystallogr F Struct Biol Commun. 2021 Jan 1;77(Pt 1):13-21. doi:, 10.1107/S2053230X20016829. Epub 2021 Jan 1. PMID:33439151^[4]

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

References

↑ Anderson KM, Berrebi-Bertrand I, Kirkpatrick RB, McQueney MS, Underwood DC, Rouanet S, Chabot-Fletcher M. cDNA sequence and characterization of the gene that encodes human myotrophin/V-1 protein, a mediator of cardiac hypertrophy. J Mol Cell Cardiol. 1999 Apr;31(4):705-19. PMID:10329199 doi:http://dx.doi.org/10.1006/jmcc.1998.0903
↑ Bhattacharya N, Ghosh S, Sept D, Cooper JA. Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end. J Biol Chem. 2006 Oct 13;281(41):31021-30. Epub 2006 Aug 7. PMID:16895918 doi:http://dx.doi.org/10.1074/jbc.M606278200
↑ Takeda S, Minakata S, Koike R, Kawahata I, Narita A, Kitazawa M, Ota M, Yamakuni T, Maeda Y, Nitanai Y. Two distinct mechanisms for actin capping protein regulation--steric and allosteric inhibition. PLoS Biol. 2010 Jul 6;8(7):e1000416. PMID:20625546 doi:10.1371/journal.pbio.1000416
↑ Takeda S, Koike R, Nagae T, Fujiwara I, Narita A, Maéda Y, Ota M. Crystal structure of human V-1 in the apo form. Acta Crystallogr F Struct Biol Commun. 2021 Jan 1;77(Pt 1):13-21. PMID:33439151 doi:10.1107/S2053230X20016829

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7df7"

Categories: Homo sapiens | Large Structures | Nagae T | Takeda S

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7df7 is ON HOLD
+==Crystal structure of human V-1 in the apo form==
+<StructureSection load='7df7' size='340' side='right'caption='[[7df7]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7df7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DF7 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=7df7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7df7 OCA], [https://pdbe.org/7df7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7df7 RCSB], [https://www.ebi.ac.uk/pdbsum/7df7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7df7 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MTPN_HUMAN MTPN_HUMAN] Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity (By similarity). Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy.<ref>PMID:10329199</ref> <ref>PMID:16895918</ref> <ref>PMID:20625546</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+V-1, also known as myotrophin, is a 13 kDa ankyrin-repeat protein that binds and inhibits the heterodimeric actin capping protein (CP), which is a key regulator of cytoskeletal actin dynamics. The crystal structure of V-1 in complex with CP revealed that V-1 recognizes CP via residues spanning several ankyrin repeats. Here, the crystal structure of human V-1 is reported in the absence of the specific ligand at 2.3 A resolution. In the asymmetric unit, the crystal contains two V-1 monomers that exhibit nearly identical structures (C(alpha) r.m.s.d. of 0.47 A). The overall structures of the two apo V-1 chains are also highly similar to that of CP-bound V-1 (C(alpha) r.m.s.d.s of &lt;0.50 A), indicating that CP does not induce a large conformational change in V-1. Detailed structural comparisons using the computational program All Atom Motion Tree revealed that CP binding can be accomplished by minor side-chain rearrangements of several residues. These findings are consistent with the known biological role of V-1, in which it globally inhibits CP in the cytoplasm.
-Authors:
+Crystal structure of human V-1 in the apo form.,Takeda S, Koike R, Nagae T, Fujiwara I, Narita A, Maeda Y, Ota M Acta Crystallogr F Struct Biol Commun. 2021 Jan 1;77(Pt 1):13-21. doi:, 10.1107/S2053230X20016829. Epub 2021 Jan 1. PMID:33439151<ref>PMID:33439151</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7df7" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Nagae T]]
+[[Category: Takeda S]]

7df7

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Current revision

Crystal structure of human V-1 in the apo form

Structural highlights

Function

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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