2h80

From Proteopedia

(Difference between revisions)

Current revision

NMR structures of SAM domain of Deleted in Liver Cancer 2 (DLC2)

Structural highlights

2h80 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.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

STA13_HUMAN GTPase-activating protein for RhoA, and perhaps for Cdc42. May be involved in regulation of cytoskeletal reorganization, cell proliferation and cell motility. Acts a tumor suppressor in hepatocellular carcinoma 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

The deleted in liver cancer 2 (DLC2) is a tumor suppressor gene, frequently found to be underexpressed in hepatocellular carcinoma. DLC2 is a multidomain protein containing a sterile alpha-motif (SAM) domain, a GTPase-activating protein (GAP) domain, and a lipid-binding StAR-related lipid-transfer (START) domain. The SAM domain of DLC2, DLC2-SAM, exhibits a low level of sequence homology (15-30%) with other SAM domains, and appears to be the prototype of a new subfamily of SAM domains found in DLC2-related proteins. In the present study, we have determined the three-dimensional solution structure of DLC2-SAM using NMR methods together with molecular dynamics simulated annealing. In addition, we performed a backbone dynamics study. The DLC2-SAM packed as a unique four alpha-helical bundle stabilized by interhelix hydrophobic interactions. The arrangement of the four helices is distinct from all other known SAM domains. In contrast to some members of the SAM domain family which form either dimers or oligomers, both biochemical analyses and rotational correlation time (tau(c)) measured by backbone 15N relaxation experiments indicated that DLC2-SAM exists as a monomer in solution. The interaction of DLC2-SAM domain with sodium dodecyl sulfate (SDS) micelles and 1,2-dimyristoyl-sn-glycerol-3-phosphatidylglycerol (DMPG) phospholipids was examined by CD and NMR spectroscopic techniques. The DLC2-SAM exhibits membrane binding properties accompanied by minor loss of the secondary structure of the protein. Deletion studies showed that the self-association of DLC2 in vivo does not require SAM domain, instead, a protein domain consisting of residues 120-672 mediates the self-association of DLC2.

Solution structures, dynamics, and lipid-binding of the sterile alpha-motif domain of the deleted in liver cancer 2.,Li H, Fung KL, Jin DY, Chung SS, Ching YP, Ng IO, Sze KH, Ko BC, Sun H Proteins. 2007 Jun 1;67(4):1154-66. PMID:17380510^[3]

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

References

↑ Nagaraja GM, Kandpal RP. Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, and yeast two-hybrid screen shows its interaction with several proteins. Biochem Biophys Res Commun. 2004 Jan 16;313(3):654-65. PMID:14697242
↑ Leung TH, Ching YP, Yam JW, Wong CM, Yau TO, Jin DY, Ng IO. Deleted in liver cancer 2 (DLC2) suppresses cell transformation by means of inhibition of RhoA activity. Proc Natl Acad Sci U S A. 2005 Oct 18;102(42):15207-12. Epub 2005 Oct 10. PMID:16217026 doi:http://dx.doi.org/10.1073/pnas.0504501102
↑ Li H, Fung KL, Jin DY, Chung SS, Ching YP, Ng IO, Sze KH, Ko BC, Sun H. Solution structures, dynamics, and lipid-binding of the sterile alpha-motif domain of the deleted in liver cancer 2. Proteins. 2007 Jun 1;67(4):1154-66. PMID:17380510 doi:http://dx.doi.org/10.1002/prot.21361

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/2h80"

@@ Line 1: / Line 1: @@
 ==NMR structures of SAM domain of Deleted in Liver Cancer 2 (DLC2)==
-<StructureSection load='2h80' size='340' side='right'caption='[[2h80]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2h80' size='340' side='right'caption='[[2h80]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2h80]] 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=2H80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H80 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2h80]] 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=2H80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H80 FirstGlance]. <br>
-</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=2h80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h80 OCA], [https://pdbe.org/2h80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h80 RCSB], [https://www.ebi.ac.uk/pdbsum/2h80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h80 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2h80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h80 OCA], [https://pdbe.org/2h80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h80 RCSB], [https://www.ebi.ac.uk/pdbsum/2h80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h80 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/STA13_HUMAN STA13_HUMAN]] GTPase-activating protein for RhoA, and perhaps for Cdc42. May be involved in regulation of cytoskeletal reorganization, cell proliferation and cell motility. Acts a tumor suppressor in hepatocellular carcinoma cells.<ref>PMID:14697242</ref> <ref>PMID:16217026</ref>
+[https://www.uniprot.org/uniprot/STA13_HUMAN STA13_HUMAN] GTPase-activating protein for RhoA, and perhaps for Cdc42. May be involved in regulation of cytoskeletal reorganization, cell proliferation and cell motility. Acts a tumor suppressor in hepatocellular carcinoma cells.<ref>PMID:14697242</ref> <ref>PMID:16217026</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Chung, S S]]
+[[Category: Chung SS]]
-[[Category: Fung, K L]]
+[[Category: Fung KL]]
-[[Category: Jin, D Y]]
+[[Category: Jin DY]]
-[[Category: Ko, B C]]
+[[Category: Ko BC]]
-[[Category: Li, H Y]]
+[[Category: Li HY]]
-[[Category: Sun, H Z]]
+[[Category: Sun HZ]]
-[[Category: Helical bundle]]
-[[Category: Lipid binding protein]]

2h80

From Proteopedia

Current revision

NMR structures of SAM domain of Deleted in Liver Cancer 2 (DLC2)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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