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.

4iqh

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:27, 23 December 2016

Crystal Structure Analysis of Dysferlin C2A variant 1 (C2Av1)

Structural highlights

4iqh is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3l9b, 2dmh, 4ihb
Gene:	DYSF, Dysferlin, FER1L1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[DYSF_HUMAN] Miyoshi myopathy;Distal myopathy with anterior tibial onset;Congenital myopathy, Paradas type;Autosomal recessive limb-girdle muscular dystrophy type 2B. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.

Function

[DYSF_HUMAN] Key calcium ion sensor involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress (By similarity).

Publication Abstract from PubMed

Dysferlin plays a critical role in the Ca2+-dependent repair of microlesions that occur in the muscle sarcolemma. Of the seven C2 domains in dysferlin, only C2A is reported to bind both Ca2+ and phospholipid, thus acting as a key sensor in membrane repair. Dysferlin C2A exists as two isoforms, the "canonical" C2A and C2A variant 1 (C2Av1). Interestingly, these isoforms have markedly different responses to Ca2+ and phospholipid. Structural and thermodynamic analyses are consistent with the canonical C2A domain as a Ca2+-dependent, phospholipid-binding domain, whereas C2Av1 would likely be Ca2+-independent under physiological conditions. Additionally, both isoforms display remarkably low free energies of stability, indicative of a highly flexible structure. The inverted ligand preference and flexibility for both C2A isoforms suggest the capability for both constitutive and Ca2+-regulated effector interactions, an activity that would be essential in its role as a mediator of membrane repair.

Alternate Splicing of Dysferlin C2A Confers Ca-Dependent and Ca-Independent Binding for Membrane Repair.,Fuson K, Rice A, Mahling R, Snow A, Nayak K, Shanbhogue P, Meyer AG, Redpath GM, Hinderliter A, Cooper ST, Sutton RB Structure. 2013 Nov 13. pii: S0969-2126(13)00392-4. doi:, 10.1016/j.str.2013.10.001. PMID:24239457^[1]

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

References

↑ Fuson K, Rice A, Mahling R, Snow A, Nayak K, Shanbhogue P, Meyer AG, Redpath GM, Hinderliter A, Cooper ST, Sutton RB. Alternate Splicing of Dysferlin C2A Confers Ca-Dependent and Ca-Independent Binding for Membrane Repair. Structure. 2013 Nov 13. pii: S0969-2126(13)00392-4. doi:, 10.1016/j.str.2013.10.001. PMID:24239457 doi:http://dx.doi.org/10.1016/j.str.2013.10.001

1 Structural highlights
2 Disease
3 Function
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/4iqh"

@@ Line 1: / Line 1: @@
 ==Crystal Structure Analysis of Dysferlin C2A variant 1 (C2Av1)==
 <StructureSection load='4iqh' size='340' side='right' caption='[[4iqh]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l9b|3l9b]], [[2dmh|2dmh]], [[4ihb|4ihb]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DYSF, Dysferlin, FER1L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4iqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iqh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4iqh RCSB], [http://www.ebi.ac.uk/pdbsum/4iqh 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=4iqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iqh OCA], [http://pdbe.org/4iqh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4iqh RCSB], [http://www.ebi.ac.uk/pdbsum/4iqh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4iqh ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4iqh" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4iqh

From Proteopedia

Revision as of 07:27, 23 December 2016

Crystal Structure Analysis of Dysferlin C2A variant 1 (C2Av1)

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox