2bex: Difference between revisions

Revision as of 19:14, 25 December 2014

CRYSTAL STRUCTURE OF PLACENTAL RIBONUCLEASE INHIBITOR IN COMPLEX WITH HUMAN EOSINOPHIL DERIVED NEUROTOXIN AT 2A RESOLUTION

Structural highlights

2bex 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:	GOL, MAK
Related:	1a4y, 1gqv, 1hi2, 1hi3, 1hi4, 1hi5, 1k2a
Activity:	Pancreatic ribonuclease, with EC number 3.1.27.5
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[RINI_HUMAN] Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis.^[1] ^[2] ^[3]

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

Placental ribonuclease inhibitor (RI) binds diverse mammalian RNases with dissociation constants that are in the femtomolar range. Previous studies on the complexes of RI with RNase A and angiogenin revealed that RI utilises largely distinctive interactions to achieve high affinity for these two ligands. Here we report a 2.0 angstroms resolution crystal structure of RI in complex with a third ligand, eosinophil-derived neurotoxin (EDN), and a mutational analysis based on this structure. The RI-EDN interface is more extensive than those of the other two complexes and contains a considerably larger set of interactions. Few of the contacts present in the RI-angiogenin complex are replicated; the correspondence to the RI-RNase A complex is somewhat greater, but still modest. The energetic contributions of various interface regions differ strikingly from those in the earlier complexes. These findings provide insight into the structural basis for the unusual combination of high avidity and relaxed stringency that RI displays.

Molecular recognition of human eosinophil-derived neurotoxin (RNase 2) by placental ribonuclease inhibitor.,Iyer S, Holloway DE, Kumar K, Shapiro R, Acharya KR J Mol Biol. 2005 Apr 1;347(3):637-55. PMID:15755456^[4]

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

References

↑ Huang GH, Yang GZ, Chen JY, Wu XF. [Expression of a human ribonuclease inhibitor variant in Escherichia coli and silkworm insect cell (Bombyx mori)]. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2003 Oct;35(10):960-3. PMID:14515218
↑ Teufel DP, Kao RY, Acharya KR, Shapiro R. Mutational analysis of the complex of human RNase inhibitor and human eosinophil-derived neurotoxin (RNase 2). Biochemistry. 2003 Feb 18;42(6):1451-9. PMID:12578357 doi:10.1021/bi026852o
↑ Monti DM, Montesano Gesualdi N, Matousek J, Esposito F, D'Alessio G. The cytosolic ribonuclease inhibitor contributes to intracellular redox homeostasis. FEBS Lett. 2007 Mar 6;581(5):930-4. Epub 2007 Feb 6. PMID:17292889 doi:10.1016/j.febslet.2007.01.072
↑ Iyer S, Holloway DE, Kumar K, Shapiro R, Acharya KR. Molecular recognition of human eosinophil-derived neurotoxin (RNase 2) by placental ribonuclease inhibitor. J Mol Biol. 2005 Apr 1;347(3):637-55. PMID:15755456 doi:10.1016/j.jmb.2005.01.035

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Huang GH, Yang GZ, Chen JY, Wu XF. [Expression of a human ribonuclease inhibitor variant in Escherichia coli and silkworm insect cell (Bombyx mori)]. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2003 Oct;35(10):960-3. PMID:14515218

[2] Teufel DP, Kao RY, Acharya KR, Shapiro R. Mutational analysis of the complex of human RNase inhibitor and human eosinophil-derived neurotoxin (RNase 2). Biochemistry. 2003 Feb 18;42(6):1451-9. PMID:12578357 doi:10.1021/bi026852o

[3] Monti DM, Montesano Gesualdi N, Matousek J, Esposito F, D'Alessio G. The cytosolic ribonuclease inhibitor contributes to intracellular redox homeostasis. FEBS Lett. 2007 Mar 6;581(5):930-4. Epub 2007 Feb 6. PMID:17292889 doi:10.1016/j.febslet.2007.01.072

[4] Iyer S, Holloway DE, Kumar K, Shapiro R, Acharya KR. Molecular recognition of human eosinophil-derived neurotoxin (RNase 2) by placental ribonuclease inhibitor. J Mol Biol. 2005 Apr 1;347(3):637-55. PMID:15755456 doi:10.1016/j.jmb.2005.01.035

[1]

[2]

[3]

[4]

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2bex]] 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=2BEX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BEX FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAK:ALPHA-KETOMALONIC+ACID'>MAK</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAK:ALPHA-KETOMALONIC+ACID'>MAK</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a4y|1a4y]], [[1gqv|1gqv]], [[1hi2|1hi2]], [[1hi3|1hi3]], [[1hi4|1hi4]], [[1hi5|1hi5]], [[1k2a|1k2a]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a4y|1a4y]], [[1gqv|1gqv]], [[1hi2|1hi2]], [[1hi3|1hi3]], [[1hi4|1hi4]], [[1hi5|1hi5]], [[1k2a|1k2a]]</td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] </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=2bex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bex OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bex RCSB], [http://www.ebi.ac.uk/pdbsum/2bex 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=2bex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bex OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bex RCSB], [http://www.ebi.ac.uk/pdbsum/2bex PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/RINI_HUMAN RINI_HUMAN]] Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis.<ref>PMID:14515218</ref> <ref>PMID:12578357</ref> <ref>PMID:17292889</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 32: @@
 *[[Ribonuclease|Ribonuclease]]
 *[[Ribonuclease inhibitor|Ribonuclease inhibitor]]
+*[[Temp|Temp]]
+*[[User:Jaime.Prilusky/Test/tree|User:Jaime.Prilusky/Test/tree]]
 == References ==
 <references/>
@@ Line 36: / Line 40: @@
 [[Category: Homo sapiens]]
 [[Category: Pancreatic ribonuclease]]
-[[Category: Acharya, K R.]]
+[[Category: Acharya, K R]]
-[[Category: Holloway, D E.]]
+[[Category: Holloway, D E]]
-[[Category: Iyer, S.]]
+[[Category: Iyer, S]]
-[[Category: Kumar, K.]]
+[[Category: Kumar, K]]
-[[Category: Shapiro, R.]]
+[[Category: Shapiro, R]]
 [[Category: Eosinophil derived neurotoxin]]
 [[Category: Hydrolase-inhibitor complex]]

2bex: Difference between revisions

Revision as of 19:14, 25 December 2014

CRYSTAL STRUCTURE OF PLACENTAL RIBONUCLEASE INHIBITOR IN COMPLEX WITH HUMAN EOSINOPHIL DERIVED NEUROTOXIN AT 2A RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools