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3b97

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Revision as of 22:25, 25 December 2014

Crystal Structure of human Enolase 1

Structural highlights

3b97 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Phosphopyruvate hydratase, with EC number 4.2.1.11
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[ENOA_HUMAN] Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production.^[1] ^[2] ^[3] ^[4] ^[5] MBP1 binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor.^[6] ^[7] ^[8] ^[9] ^[10]

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

Aside from its enzymatic function in the glycolytic pathway, alpha-enolase (ENO1) has been implicated in numerous diseases, including metastatic cancer, autoimmune disorders, ischaemia and bacterial infection. The disease-related roles of ENO1 are mostly attributed to its immunogenic capacity, DNA-binding ability and plasmin(ogen) receptor function, which are significantly affected by its three-dimensional structure and surface properties, rather than its enzymatic activity. Here, the crystal structure of human ENO1 (hENO1) is presented at 2.2 A resolution. Despite its high sequence similarity to other enolases, the hENO1 structure exhibits distinct surface properties, explaining its various activities, including plasmin(ogen) and DNA binding.

Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme.,Kang HJ, Jung SK, Kim SJ, Chung SJ Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):651-7. Epub 2008, May 14. PMID:18560153^[11]

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

References

↑ Ray R, Miller DM. Cloning and characterization of a human c-myc promoter-binding protein. Mol Cell Biol. 1991 Apr;11(4):2154-61. PMID:2005901
↑ Sugahara T, Nakajima H, Shirahata S, Murakami H. Purification and characterization of immunoglobulin production stimulating factor-II beta derived from Namalwa cells. Cytotechnology. 1992;10(2):137-46. PMID:1369209
↑ Ghosh AK, Steele R, Ray RB. Functional domains of c-myc promoter binding protein 1 involved in transcriptional repression and cell growth regulation. Mol Cell Biol. 1999 Apr;19(4):2880-6. PMID:10082554
↑ Feo S, Arcuri D, Piddini E, Passantino R, Giallongo A. ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1). FEBS Lett. 2000 May 4;473(1):47-52. PMID:10802057
↑ Lopez-Alemany R, Longstaff C, Hawley S, Mirshahi M, Fabregas P, Jardi M, Merton E, Miles LA, Felez J. Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against alpha-Enolase. Am J Hematol. 2003 Apr;72(4):234-42. PMID:12666133 doi:http://dx.doi.org/10.1002/ajh.10299
↑ Ray R, Miller DM. Cloning and characterization of a human c-myc promoter-binding protein. Mol Cell Biol. 1991 Apr;11(4):2154-61. PMID:2005901
↑ Sugahara T, Nakajima H, Shirahata S, Murakami H. Purification and characterization of immunoglobulin production stimulating factor-II beta derived from Namalwa cells. Cytotechnology. 1992;10(2):137-46. PMID:1369209
↑ Ghosh AK, Steele R, Ray RB. Functional domains of c-myc promoter binding protein 1 involved in transcriptional repression and cell growth regulation. Mol Cell Biol. 1999 Apr;19(4):2880-6. PMID:10082554
↑ Feo S, Arcuri D, Piddini E, Passantino R, Giallongo A. ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1). FEBS Lett. 2000 May 4;473(1):47-52. PMID:10802057
↑ Lopez-Alemany R, Longstaff C, Hawley S, Mirshahi M, Fabregas P, Jardi M, Merton E, Miles LA, Felez J. Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against alpha-Enolase. Am J Hematol. 2003 Apr;72(4):234-42. PMID:12666133 doi:http://dx.doi.org/10.1002/ajh.10299
↑ Kang HJ, Jung SK, Kim SJ, Chung SJ. Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme. Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):651-7. Epub 2008, May 14. PMID:18560153 doi:10.1107/S0907444908008561

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3b97"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[3b97]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B97 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3B97 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b97 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3b97 RCSB], [http://www.ebi.ac.uk/pdbsum/3b97 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=3b97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b97 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3b97 RCSB], [http://www.ebi.ac.uk/pdbsum/3b97 PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ENOA_HUMAN ENOA_HUMAN]] Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production.<ref>PMID:2005901</ref> <ref>PMID:1369209</ref> <ref>PMID:10082554</ref> <ref>PMID:10802057</ref> <ref>PMID:12666133</ref>   MBP1 binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor.<ref>PMID:2005901</ref> <ref>PMID:1369209</ref> <ref>PMID:10082554</ref> <ref>PMID:10802057</ref> <ref>PMID:12666133</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 36: @@
 [[Category: Homo sapiens]]
 [[Category: Phosphopyruvate hydratase]]
-[[Category: Chung, S J.]]
+[[Category: Chung, S J]]
-[[Category: Jung, S K.]]
+[[Category: Jung, S K]]
-[[Category: Kang, H J.]]
+[[Category: Kang, H J]]
-[[Category: Kim, S J.]]
+[[Category: Kim, S J]]
 [[Category: Alpha/beta hydrolase]]
 [[Category: Alternative initiation]]

3b97

From Proteopedia

Revision as of 22:25, 25 December 2014

Crystal Structure of human Enolase 1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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