This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1lpl

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:47, 31 January 2018

Structural Genomics of Caenorhabditis elegans: CAP-Gly domain of F53F4.3

Structural highlights

1lpl is a 1 chain structure with sequence from Caeel. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	F53F4.3 (CAEEL)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[TBCB_CAEEL] Binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway leading from newly synthesized tubulin to properly folded heterodimer.

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

Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of the CAP-Gly domain of Caenorhabditis elegans F53F4.3 protein, solved by single wavelength sulfur-anomalous phasing, revealed a novel protein fold containing three beta-sheets. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Residues in the groove are highly conserved as measured from the information content of the aligned sequences. The C-terminal tail of another molecule in the crystal is bound in this groove.

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain.,Li S, Finley J, Liu ZJ, Qiu SH, Chen H, Luan CH, Carson M, Tsao J, Johnson D, Lin G, Zhao J, Thomas W, Nagy LA, Sha B, DeLucas LJ, Wang BC, Luo M J Biol Chem. 2002 Dec 13;277(50):48596-601. Epub 2002 Sep 7. PMID:12221106^[1]

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

References

↑ Li S, Finley J, Liu ZJ, Qiu SH, Chen H, Luan CH, Carson M, Tsao J, Johnson D, Lin G, Zhao J, Thomas W, Nagy LA, Sha B, DeLucas LJ, Wang BC, Luo M. Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain. J Biol Chem. 2002 Dec 13;277(50):48596-601. Epub 2002 Sep 7. PMID:12221106 doi:http://dx.doi.org/10.1074/jbc.M208512200

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/1lpl"

@@ Line 1: / Line 1: @@
 ==Structural Genomics of Caenorhabditis elegans: CAP-Gly domain of F53F4.3==
 <StructureSection load='1lpl' size='340' side='right' caption='[[1lpl]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1lpl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LPL FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">F53F4.3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=1lpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lpl OCA], [http://pdbe.org/1lpl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lpl RCSB], [http://www.ebi.ac.uk/pdbsum/1lpl PDBsum], [http://www.topsan.org/Proteins/SECSG/1lpl TOPSAN]</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=1lpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lpl OCA], [http://pdbe.org/1lpl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lpl RCSB], [http://www.ebi.ac.uk/pdbsum/1lpl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lpl ProSAT], [http://www.topsan.org/Proteins/SECSG/1lpl TOPSAN]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lp/1lpl_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lp/1lpl_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 31: @@
 ==See Also==
 *[[CAP-Gly domain|CAP-Gly domain]]
-*[[CAP-Gly domain of F53F4.3|CAP-Gly domain of F53F4.3]]
 == References ==
 <references/>

1lpl

From Proteopedia

Revision as of 07:47, 31 January 2018

Structural Genomics of Caenorhabditis elegans: CAP-Gly domain of F53F4.3

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox