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1a33

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Revision as of 10:46, 8 November 2017

PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI

Structural highlights

1a33 is a 1 chain structure with sequence from Bruma. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	BMCYP-1 (BRUMA)
Activity:	Peptidylprolyl isomerase, with EC number 5.2.1.8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CYP1_BRUMA] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

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

Cyclophilins are a family of proteins that exhibit peptidyl-prolyl cis-trans isomerase activity and bind the immunosuppressive agent cyclosporin A (CsA). Brugia malayi is a filarial nematode parasite of humans, for which a cyclophilin-like domain was identified at the N-terminal of a protein containing 843 amino acid residues. There are two differences in sequence in the highly conserved CsA binding site: A histidine and a lysine replace a tryptophan and an alanine, respectively. The crystal structure of this domain has been determined by the molecular replacement method and refined to an R-factor of 16.9% at 2.15 A resolution. The overall structure is similar to other cyclophilins; however, major differences occur in two loops. Comparison of the CsA binding site of this domain with members of the cyclophilin family shows significant structural differences, which can account for the reduced sensitivity of the Brugia malayi protein to inhibition by CsA.

Crystal structure of the cyclophilin-like domain from the parasitic nematode Brugia malayi.,Mikol V, Ma D, Carlow CK Protein Sci. 1998 Jun;7(6):1310-6. PMID:9655334^[1]

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

References

↑ Mikol V, Ma D, Carlow CK. Crystal structure of the cyclophilin-like domain from the parasitic nematode Brugia malayi. Protein Sci. 1998 Jun;7(6):1310-6. PMID:9655334 doi:10.1002/pro.5560070606

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/1a33"

@@ Line 1: / Line 1: @@
 ==PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI==
 <StructureSection load='1a33' size='340' side='right' caption='[[1a33]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMCYP-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6279 BRUMA])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=1a33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a33 OCA], [http://pdbe.org/1a33 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a33 RCSB], [http://www.ebi.ac.uk/pdbsum/1a33 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=1a33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a33 OCA], [http://pdbe.org/1a33 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a33 RCSB], [http://www.ebi.ac.uk/pdbsum/1a33 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a33 ProSAT]</span></td></tr>
 </table>
 == Function ==

1a33

From Proteopedia

Revision as of 10:46, 8 November 2017

PEPTIDYLPROLYL ISOMERASE, CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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