|
|
| (2 intermediate revisions not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='1rc9' size='340' side='right'caption='[[1rc9]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='1rc9' size='340' side='right'caption='[[1rc9]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rc9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chinese_green_tree_viper Chinese green tree viper]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RC9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rc9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trimeresurus_stejnegeri Trimeresurus stejnegeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RC9 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=1rc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rc9 OCA], [http://pdbe.org/1rc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rc9 RCSB], [http://www.ebi.ac.uk/pdbsum/1rc9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rc9 ProSAT]</span></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]] 1.6Å</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=1rc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rc9 OCA], [https://pdbe.org/1rc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rc9 RCSB], [https://www.ebi.ac.uk/pdbsum/1rc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rc9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CRVP_TRIST CRVP_TRIST]] Blocks contraction of smooth muscle elicited by high potassium-induced depolarization, but does not block caffein-stimulated contraction. May target voltage-gated calcium channels on smooth muscle (By similarity). | + | [https://www.uniprot.org/uniprot/CRVP_TRIST CRVP_TRIST] Blocks contraction of smooth muscle elicited by high potassium-induced depolarization, but does not block caffein-stimulated contraction. May target voltage-gated calcium channels on smooth muscle (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 13: |
Line 14: |
| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rc/1rc9_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rc/1rc9_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
| Line 31: |
Line 32: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chinese green tree viper]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Guo, M]] | + | [[Category: Trimeresurus stejnegeri]] |
| - | [[Category: Niu, L]] | + | [[Category: Guo M]] |
| - | [[Category: Teng, M]]
| + | [[Category: Niu L]] |
| - | [[Category: Beta-alpha sandwich]] | + | [[Category: Teng M]] |
| - | [[Category: Double domain]] | + | |
| - | [[Category: Short helixs motif]]
| + | |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
CRVP_TRIST Blocks contraction of smooth muscle elicited by high potassium-induced depolarization, but does not block caffein-stimulated contraction. May target voltage-gated calcium channels on smooth muscle (By similarity).
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
Stecrisp from Trimeresurus stejnegeri snake venom belongs to a family of cysteine-rich secretory proteins (CRISP) that have various functions related to sperm-egg fusion, innate host defense, and the blockage of ion channels. Here we present the crystal structure of stecrisp refined to 1.6-angstrom resolution. It shows that stecrisp contains three regions, namely a PR-1 (pathogenesis-related proteins of group1) domain, a hinge, and a cysteine-rich domain (CRD). A conformation of solvent-exposed and -conserved residues (His60, Glu75, Glu96, and His115) in the PR-1 domain similar to that of their counterparts in homologous structures suggests they may share some molecular mechanism. Three flexible loops of hypervariable sequence surrounding the possible substrate binding site in the PR-1 domain show an evident difference in homologous structures, implying that a great diversity of species- and substrate-specific interactions may be involved in recognition and catalysis. The hinge is fixed by two crossed disulfide bonds formed by four of ten characteristic cysteines in the carboxyl-terminal region and is important for stabilizing the N-terminal PR-1 domain. Spatially separated from the PR-1 domain, CRD possesses a similar fold with two K+ channel inhibitors (Bgk and Shk). Several candidates for the possible functional sites of ion channel blocking are located in a solvent-exposed loop in the CRD. The structure of stecrisp will provide a prototypic architecture for a structural and functional exploration of the diverse members of the CRISP family.
Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel inhibitor-like fold.,Guo M, Teng M, Niu L, Liu Q, Huang Q, Hao Q J Biol Chem. 2005 Apr 1;280(13):12405-12. Epub 2004 Dec 13. PMID:15596436[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guo M, Teng M, Niu L, Liu Q, Huang Q, Hao Q. Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel inhibitor-like fold. J Biol Chem. 2005 Apr 1;280(13):12405-12. Epub 2004 Dec 13. PMID:15596436 doi:10.1074/jbc.M413566200
|
