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2lv7

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Revision as of 13:12, 22 February 2023

Solution structure of Ca2+-bound CaBP7 N-terminal doman

Structural highlights

2lv7 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CABP7_HUMAN Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity.

Publication Abstract from PubMed

Calcium-binding protein 7 (CaBP7) is a member of the calmodulin (CaM) superfamily that harbors two high affinity EF-hand motifs and a C-terminal transmembrane domain. CaBP7 has been previously shown to interact with and modulate phosphatidylinositol 4-kinase III-beta (PI4KIIIbeta) activity in in vitro assays and affects vesicle transport in neurons when overexpressed. Here we show that the N-terminal domain (NTD) of CaBP7 is sufficient to mediate the interaction of CaBP7 with PI4KIIIbeta. CaBP7 NTD encompasses the two high affinity Ca(2+) binding sites, and structural characterization through multiangle light scattering, circular dichroism, and NMR reveals unique properties for this domain. CaBP7 NTD binds specifically to Ca(2+) but not Mg(2+) and undergoes significant conformational changes in both secondary and tertiary structure upon Ca(2+) binding. The Ca(2+)-bound form of CaBP7 NTD is monomeric and exhibits an open conformation similar to that of CaM. Ca(2+)-bound CaBP7 NTD has a solvent-exposed hydrophobic surface that is more expansive than observed in CaM or CaBP1. Within this hydrophobic pocket, there is a significant reduction in the number of methionine residues that are conserved in CaM and CaBP1 and shown to be important for target recognition. In CaBP7 NTD, these residues are replaced with isoleucine and leucine residues with branched side chains that are intrinsically more rigid than the flexible methionine side chain. We propose that these differences in surface hydrophobicity, charge, and methionine content may be important in determining highly specific interactions of CaBP7 with target proteins, such as PI4KIIIbeta.

Solution NMR Structure of the Ca2+-bound N-terminal Domain of CaBP7: A REGULATOR OF GOLGI TRAFFICKING.,McCue HV, Patel P, Herbert AP, Lian LY, Burgoyne RD, Haynes LP J Biol Chem. 2012 Nov 2;287(45):38231-43. doi: 10.1074/jbc.M112.402289. Epub 2012, Sep 18. PMID:22989873^[1]

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

References

↑ McCue HV, Patel P, Herbert AP, Lian LY, Burgoyne RD, Haynes LP. Solution NMR Structure of the Ca2+-bound N-terminal Domain of CaBP7: A REGULATOR OF GOLGI TRAFFICKING. J Biol Chem. 2012 Nov 2;287(45):38231-43. doi: 10.1074/jbc.M112.402289. Epub 2012, Sep 18. PMID:22989873 doi:http://dx.doi.org/10.1074/jbc.M112.402289

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/2lv7"

@@ Line 1: / Line 1: @@
 ==Solution structure of Ca2+-bound CaBP7 N-terminal doman==
-<StructureSection load='2lv7' size='340' side='right'caption='[[2lv7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2lv7' size='340' side='right'caption='[[2lv7]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2lv7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LV7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2lv7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LV7 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CABP7, CALN2 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2lv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lv7 OCA], [https://pdbe.org/2lv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lv7 RCSB], [https://www.ebi.ac.uk/pdbsum/2lv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lv7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CABP7_HUMAN CABP7_HUMAN]] Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity.
+[https://www.uniprot.org/uniprot/CABP7_HUMAN CABP7_HUMAN] Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Burgoyne, R D]]
+[[Category: Burgoyne RD]]
-[[Category: Haynes, L P]]
+[[Category: Haynes LP]]
-[[Category: Herbert, A P]]
+[[Category: Herbert AP]]
-[[Category: Lian, L]]
+[[Category: Lian L]]
-[[Category: Mccue, H V]]
+[[Category: Mccue HV]]
-[[Category: Patel, P]]
+[[Category: Patel P]]
-[[Category: Calcium-binding protein]]
-[[Category: Metal binding protein]]

2lv7

From Proteopedia

Revision as of 13:12, 22 February 2023

Solution structure of Ca2+-bound CaBP7 N-terminal doman

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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