1g2b

From Proteopedia

(Difference between revisions)

@@ Line 1: / Line 1: @@
 ==ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT N47-D48==
-<StructureSection load='1g2b' size='340' side='right' caption='[[1g2b]], [[Resolution|resolution]] 1.12&Aring;' scene=''>
+<StructureSection load='1g2b' size='340' side='right'caption='[[1g2b]], [[Resolution|resolution]] 1.12&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1g2b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G2B FirstGlance]. <br>
@@ Line 13: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g2/1g2b_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g2/1g2b_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 36: / Line 36: @@
 </StructureSection>
 [[Category: Chick]]
+[[Category: Large Structures]]
 [[Category: Berisio, R]]
 [[Category: Serrano, L]]

Revision as of 07:19, 10 July 2019

ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT N47-D48

spinqualitylabelsall models

PDB ID 1g2b

Show:Asymmetric Unit Biological Assembly

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Structural highlights

1g2b is a 1 chain structure with sequence from Chick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SPTN1_CHICK] Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.

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

The crystal structure of an alpha-spectrin Src-homology 3 (SH3) domain mutant has been refined at 1.12 A resolution. This X-ray structure is at the highest resolution achieved so far for an SH3 domain. The structure allows the identification of a complete set of specific interactions and is useful for the elucidation of relations between structure and pH-dependent thermodynamic stability in a series of SH3 domain mutants.

Atomic resolution structure of a mutant of the spectrin SH3 domain.,Berisio R, Viguera A, Serrano L, Wilmanns M Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):337-40. PMID:11173498^[1]

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

References

↑ Berisio R, Viguera A, Serrano L, Wilmanns M. Atomic resolution structure of a mutant of the spectrin SH3 domain. Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):337-40. PMID:11173498

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

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1g2b

From Proteopedia

Revision as of 07:19, 10 July 2019

ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT N47-D48

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

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Proteopedia Page Contributors and Editors (what is this?)

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