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1xta

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Revision as of 16:19, 3 November 2021

Crystal Structure of Natrin, a snake venom CRISP from Taiwan cobra (Naja atra)

Structural highlights

1xta is a 2 chain structure with sequence from Naja atra. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CRVP1_NAJAT] Inhibits calcium-activated potassium channels (KCa1.1/KCNMA1), voltage-gated potassium channel Kv1.3/KCNA3, and the calcium release channel/ryanodine receptor (RyR). Binds specifically to type 1 RyR (RyR1) from skeletal muscle. Inhibit both the binding of ryanodine to RyR1, and RyR1's calcium-channel activity. Inhibits carbachol-induced muscle contraction and weakly blocks muscle contraction evoked by potassium.^[1] ^[2] ^[3] ^[4]

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

Cysteine-rich secretory proteins (CRISPs) play an important role in the innate immune system and are transcriptionally regulated by androgens in several tissues. The proteins are mostly found in the epididymis and granules of mammals, whilst a number of snake venoms also contain CRISP-family proteins. The natrin protein from the venom of Naja atra (Taiwan cobra), which belongs to a family of CRISPs and has a cysteine-rich C-terminal amino-acid sequence, has been purified using a three-stage chromatography procedure and crystals suitable for X-ray analysis have been obtained using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 1.58 A resolution using synchrotron radiation; the crystals belong to space group C222(1), with unit-cell parameters a = 59.172, b = 65.038, c = 243.156 A. There are two protein molecules in the asymmetric unit and the Matthews coefficient is estimated to be 2.35 A3 Da(-1), corresponding to a solvent content of 47.60%.

Purification, crystallization and preliminary X-ray crystallographic analysis of a cysteine-rich secretory protein (CRISP) from Naja atra venom.,Wang YL, Goh KX, Wu WG, Chen CJ Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1912-5. Epub 2004, Sep 23. PMID:15388950^[5]

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

References

↑ Chang LS, Liou JC, Lin SR, Cheng YC. Purification and characterization of Taiwan cobra venom proteins with weak toxicity. Toxicon. 2005 Jan;45(1):21-5. PMID:15581679 doi:10.1016/j.toxicon.2004.09.002
↑ Wang F, Li H, Liu MN, Song H, Han HM, Wang QL, Yin CC, Zhou YC, Qi Z, Shu YY, Lin ZJ, Jiang T. Structural and functional analysis of natrin, a venom protein that targets various ion channels. Biochem Biophys Res Commun. 2006 Dec 15;351(2):443-8. Epub 2006 Oct 20. PMID:17070778 doi:10.1016/j.bbrc.2006.10.067
↑ Zhou Q, Wang QL, Meng X, Shu Y, Jiang T, Wagenknecht T, Yin CC, Sui SF, Liu Z. Structural and functional characterization of ryanodine receptor-natrin toxin interaction. Biophys J. 2008 Nov 1;95(9):4289-99. doi: 10.1529/biophysj.108.137224. Epub 2008 , Jul 25. PMID:18658224 doi:10.1529/biophysj.108.137224
↑ Wang J, Shen B, Guo M, Lou X, Duan Y, Cheng XP, Teng M, Niu L, Liu Q, Huang Q, Hao Q. Blocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from Naja atra venom that targets the BKCa channel. Biochemistry. 2005 Aug 2;44(30):10145-52. PMID:16042391 doi:10.1021/bi050614m
↑ Wang YL, Goh KX, Wu WG, Chen CJ. Purification, crystallization and preliminary X-ray crystallographic analysis of a cysteine-rich secretory protein (CRISP) from Naja atra venom. Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1912-5. Epub 2004, Sep 23. PMID:15388950 doi:10.1107/S0907444904019766

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/1xta"

@@ Line 3: / Line 3: @@
 <StructureSection load='1xta' size='340' side='right'caption='[[1xta]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xta]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XTA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XTA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xta]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XTA FirstGlance]. <br>
-</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=1xta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xta OCA], [http://pdbe.org/1xta PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xta RCSB], [http://www.ebi.ac.uk/pdbsum/1xta PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xta ProSAT]</span></td></tr>
+</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=1xta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xta OCA], [https://pdbe.org/1xta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xta RCSB], [https://www.ebi.ac.uk/pdbsum/1xta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xta ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CRVP1_NAJAT CRVP1_NAJAT]] Inhibits calcium-activated potassium channels (KCa1.1/KCNMA1), voltage-gated potassium channel Kv1.3/KCNA3, and the calcium release channel/ryanodine receptor (RyR). Binds specifically to type 1 RyR (RyR1) from skeletal muscle. Inhibit both the binding of ryanodine to RyR1, and RyR1's calcium-channel activity. Inhibits carbachol-induced muscle contraction and weakly blocks muscle contraction evoked by potassium.<ref>PMID:15581679</ref> <ref>PMID:17070778</ref> <ref>PMID:18658224</ref> <ref>PMID:16042391</ref>
+[[https://www.uniprot.org/uniprot/CRVP1_NAJAT CRVP1_NAJAT]] Inhibits calcium-activated potassium channels (KCa1.1/KCNMA1), voltage-gated potassium channel Kv1.3/KCNA3, and the calcium release channel/ryanodine receptor (RyR). Binds specifically to type 1 RyR (RyR1) from skeletal muscle. Inhibit both the binding of ryanodine to RyR1, and RyR1's calcium-channel activity. Inhibits carbachol-induced muscle contraction and weakly blocks muscle contraction evoked by potassium.<ref>PMID:15581679</ref> <ref>PMID:17070778</ref> <ref>PMID:18658224</ref> <ref>PMID:16042391</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1xta

From Proteopedia

Revision as of 16:19, 3 November 2021

Crystal Structure of Natrin, a snake venom CRISP from Taiwan cobra (Naja atra)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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