2v77

From Proteopedia

(Difference between revisions)

Revision as of 15:08, 13 December 2023

Crystal Structure of Human Carboxypeptidase A1

Structural highlights

2v77 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 1.603Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBPA1_HUMAN Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.^[1]

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

Carboxypeptidase A1 has been the subject of extensive research in the last 30 y and is one of the most widely studied zinc metalloenzymes. However, the three-dimensional structure of the human form of the enzyme is not yet available. This report describes the three-dimensional structure of human carboxypeptidase A1 (hCPA1) derived from crystals that belong to the tetragonal space group P4(3)2(1)2 and diffract to 1.6 angstroms resolution. A description of the ternary complex hCPA1-Zn2+-poly(acrylic acid) is included as a model of the interaction of mucoadhesive polymers with proteases in the gastrointestinal tract. The direct mode of interaction between poly(acrylic acid) and the active site of the target protease was confirmed by in vitro inhibition assays. The structure was further analyzed in silico through the optimal docking-area method. The characterization of binding sites on the surface of hCPA1 and a comparison with other available carboxypeptidase structures provided further insights into the formation of multiprotein complexes and the activation mechanisms of carboxypeptidase zymogens. The high-resolution structure of hCPA1 provides an excellent template for the modelling of physiologically relevant carboxypeptidases and could also contribute to the design of specific agents for biomedical purposes.

Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid).,Pallares I, Fernandez D, Comellas-Bigler M, Fernandez-Recio J, Ventura S, Aviles FX, Bode W, Vendrell J Acta Crystallogr D Biol Crystallogr. 2008 Jul;D64(Pt 7):784-91. Epub 2008, Jun 18. PMID:18566513^[2]

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

References

↑ Laethem RM, Blumenkopf TA, Cory M, Elwell L, Moxham CP, Ray PH, Walton LM, Smith GK. Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2. Arch Biochem Biophys. 1996 Aug 1;332(1):8-18. PMID:8806703 doi:http://dx.doi.org/S0003-9861(96)90310-0
↑ Pallares I, Fernandez D, Comellas-Bigler M, Fernandez-Recio J, Ventura S, Aviles FX, Bode W, Vendrell J. Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid). Acta Crystallogr D Biol Crystallogr. 2008 Jul;D64(Pt 7):784-91. Epub 2008, Jun 18. PMID:18566513 doi:10.1107/S0907444908013474

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/2v77"

@@ Line 3: / Line 3: @@
 <StructureSection load='2v77' size='340' side='right'caption='[[2v77]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2v77]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V77 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2v77]] 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=2V77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V77 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=PAY:OCTANE-1,3,5,7-TETRACARBOXYLIC+ACID'>PAY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.603&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.14.17.1 3.14.17.1] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=PAY:OCTANE-1,3,5,7-TETRACARBOXYLIC+ACID'>PAY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2v77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v77 OCA], [https://pdbe.org/2v77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v77 RCSB], [https://www.ebi.ac.uk/pdbsum/2v77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v77 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CBPA1_HUMAN CBPA1_HUMAN]] Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.<ref>PMID:8806703</ref>
+[https://www.uniprot.org/uniprot/CBPA1_HUMAN CBPA1_HUMAN] Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.<ref>PMID:8806703</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Hydrolase]]
 [[Category: Large Structures]]
-[[Category: Aviles, F X]]
+[[Category: Aviles FX]]
-[[Category: Comellas-Bigler, M]]
+[[Category: Comellas-Bigler M]]
-[[Category: Fernandez, D]]
+[[Category: Fernandez D]]
-[[Category: Fernandez-Recio, J]]
+[[Category: Fernandez-Recio J]]
-[[Category: Pallares, I]]
+[[Category: Pallares I]]
-[[Category: Vendrell, J]]
+[[Category: Vendrell J]]
-[[Category: Ventura, S]]
+[[Category: Ventura S]]
-[[Category: Carboxypeptidase]]
-[[Category: Metal-binding]]
-[[Category: Metalloprotease]]
-[[Category: Protease]]
-[[Category: Protein degradation]]
-[[Category: Secreted]]
-[[Category: Zinc]]
-[[Category: Zymogen]]

2v77

From Proteopedia

Revision as of 15:08, 13 December 2023

Crystal Structure of Human Carboxypeptidase A1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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