2m99

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of a chymotrypsin inhibitor from the Taiwan cobra

Structural highlights

2m99 is a 1 chain structure with sequence from Naja atra. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 20 models
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VKT_NAJAT Serine protease inhibitor that inhibits chymotrypsin (Ki=25 nM) (PubMed:14990218, PubMed:15698956). Also interacts with vasopressin V2 receptor (V2R/AVPR2) (PubMed:35122240). Inhibits vasopressin binding human V2R in the nanomolar range (Ki=112 nM), and also moderately inhibits vasopressin-induced cAMP production (IC(50)=138 nM). In vivo, intraperitoneal injection of this protein into rats increases diuresis by 2.2-fold, without any loss of electrolytes (PubMed:35122240).^[1] ^[2] ^[3]

Publication Abstract from PubMed

The Taiwan cobra (Naja naja atra) chymotrypsin inhibitor (NACI) consists of 57 amino acids and is related to other Kunitz-type inhibitors such as bovine pancreatic trypsin inhibitor (BPTI) and Bungarus fasciatus fraction IX (BF9), another chymotrypsin inhibitor. Here we present the solution structure of NACI. We determined the NMR structure of NACI with a root-mean-square deviation of 0.37 A for the backbone atoms and 0.73 A for the heavy atoms on the basis of 1,075 upper distance limits derived from NOE peaks measured in its NOESY spectra. To investigate the structural characteristics of NACI, we compared the three-dimensional structure of NACI with BPTI and BF9. The structure of the NACI protein comprises one 310-helix, one alpha-helix and one double-stranded antiparallel beta-sheet, which is comparable with the secondary structures in BPTI and BF9. The RMSD value between the mean structures is 1.09 A between NACI and BPTI and 1.27 A between NACI and BF9. In addition to similar secondary and tertiary structure, NACI might possess similar types of protein conformational fluctuations as reported in BPTI, such as Cys14-Cys38 disulfide bond isomerization, based on line broadening of resonances from residues which are mainly confined to a region around the Cys14-Cys38 disulfide bond.

NMR solution structure of a Chymotrypsin inhibitor from the Taiwan cobra Naja naja atra.,Lin YJ, Ikeya T, Guntert P, Chang LS Molecules. 2013 Jul 26;18(8):8906-18. doi: 10.3390/molecules18088906. PMID:23896616^[4]

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

References

↑ Zhou XD, Jin Y, Lu QM, Li DS, Zhu SW, Wang WY, Xiong YL. Purification, characterization and primary structure of a chymotrypsin inhibitor from Naja atra venom. Comp Biochem Physiol B Biochem Mol Biol. 2004 Feb;137(2):219-24. PMID:14990218 doi:10.1016/j.cbpc.2003.11.007
↑ Cheng YC, Yan FJ, Chang LS. Taiwan cobra chymotrypsin inhibitor: cloning, functional expression and gene organization. Biochim Biophys Acta. 2005 Mar 14;1747(2):213-20. PMID:15698956 doi:10.1016/j.bbapap.2004.11.006
↑ Droctové L, Ciolek J, Mendre C, Chorfa A, Huerta P, Carvalho C, Gouin C, Lancien M, Stanajic-Petrovic G, Braco L, Blanchet G, Upert G, De Pauw G, Barbe P, Keck M, Mourier G, Mouillac B, Denis S, Rodríguez de la Vega RC, Quinton L, Gilles N. A new Kunitz-type snake toxin family associated with an original mode of interaction with the vasopressin 2 receptor. Br J Pharmacol. 2022 Jul;179(13):3470-3481. PMID:35122240 doi:10.1111/bph.15814
↑ Lin YJ, Ikeya T, Guntert P, Chang LS. NMR solution structure of a Chymotrypsin inhibitor from the Taiwan cobra Naja naja atra. Molecules. 2013 Jul 26;18(8):8906-18. doi: 10.3390/molecules18088906. PMID:23896616 doi:http://dx.doi.org/10.3390/molecules18088906

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2m99"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2m99 is ON HOLD
+==Solution structure of a chymotrypsin inhibitor from the Taiwan cobra==
+<StructureSection load='2m99' size='340' side='right'caption='[[2m99]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2m99]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M99 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2m99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m99 OCA], [https://pdbe.org/2m99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m99 RCSB], [https://www.ebi.ac.uk/pdbsum/2m99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m99 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/VKT_NAJAT VKT_NAJAT] Serine protease inhibitor that inhibits chymotrypsin (Ki=25 nM) (PubMed:14990218, PubMed:15698956). Also interacts with vasopressin V2 receptor (V2R/AVPR2) (PubMed:35122240). Inhibits vasopressin binding human V2R in the nanomolar range (Ki=112 nM), and also moderately inhibits vasopressin-induced cAMP production (IC(50)=138 nM). In vivo, intraperitoneal injection of this protein into rats increases diuresis by 2.2-fold, without any loss of electrolytes (PubMed:35122240).<ref>PMID:14990218</ref> <ref>PMID:15698956</ref> <ref>PMID:35122240</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The Taiwan cobra (Naja naja atra) chymotrypsin inhibitor (NACI) consists of 57 amino acids and is related to other Kunitz-type inhibitors such as bovine pancreatic trypsin inhibitor (BPTI) and Bungarus fasciatus fraction IX (BF9), another chymotrypsin inhibitor. Here we present the solution structure of NACI. We determined the NMR structure of NACI with a root-mean-square deviation of 0.37 A for the backbone atoms and 0.73 A for the heavy atoms on the basis of 1,075 upper distance limits derived from NOE peaks measured in its NOESY spectra. To investigate the structural characteristics of NACI, we compared the three-dimensional structure of NACI with BPTI and BF9. The structure of the NACI protein comprises one 310-helix, one alpha-helix and one double-stranded antiparallel beta-sheet, which is comparable with the secondary structures in BPTI and BF9. The RMSD value between the mean structures is 1.09 A between NACI and BPTI and 1.27 A between NACI and BF9. In addition to similar secondary and tertiary structure, NACI might possess similar types of protein conformational fluctuations as reported in BPTI, such as Cys14-Cys38 disulfide bond isomerization, based on line broadening of resonances from residues which are mainly confined to a region around the Cys14-Cys38 disulfide bond.
-Authors: Lin, Y.-J., Ikeya, T., Guntert, P., Chang, L.-S.
+NMR solution structure of a Chymotrypsin inhibitor from the Taiwan cobra Naja naja atra.,Lin YJ, Ikeya T, Guntert P, Chang LS Molecules. 2013 Jul 26;18(8):8906-18. doi: 10.3390/molecules18088906. PMID:23896616<ref>PMID:23896616</ref>
-Description: Solution structure of a chymotrypsin inhibitor from the Taiwan cobra
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2m99" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Naja atra]]
+[[Category: Chang L-S]]
+[[Category: Guntert P]]
+[[Category: Ikeya T]]
+[[Category: Lin Y-J]]

2m99

From Proteopedia

Current revision

Solution structure of a chymotrypsin inhibitor from the Taiwan cobra

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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