1y1a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:54, 14 February 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1y1a.gif|left|200px]]<br /><applet load="1y1a" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1y1a, resolution 2.30&Aring;" />
 
-
'''CRYSTAL STRUCTURE OF CALCIUM AND INTEGRIN BINDING PROTEIN'''<br />
 
-
==Overview==
+
==CRYSTAL STRUCTURE OF CALCIUM AND INTEGRIN BINDING PROTEIN==
-
Calcium- and integrin-binding protein 1 (CIB1) is involved in the process, of platelet aggregation by binding the cytoplasmic tail of the alpha(IIb), subunit of the platelet-specific integrin alpha(Iib)beta(3). Although, poorly understood, it is widely believed that CIB1 acts as a global, signaling regulator because it is expressed in many tissues that do not, express integrin alpha(Iib)beta(3). We report the structure of human CIB1, to a resolution of 2.3 A, crystallized as a dimer. The dimer interface, includes an extensive hydrophobic patch in a crystal form with 80% solvent, content. Although the dimer form of CIB1 may not be physiologically, relevant, this intersub-unit surface is likely to be linked to alpha(IIb), binding and to the binding of other signaling partner proteins. The, C-terminal domain of CIB1 is structurally similar to other EF-hand, proteins such as calmodulin and calcineurin B. Despite structural homology, to the C-terminal domain, the N-terminal domain of CIB1 lacks, calcium-binding sites. The structure of CIB1 revealed a complex with a, molecule of glutathione in the reduced state bond to the N-terminal domain, of one of the two subunits poised to interact with the free thiol of C35., Glutathione bound in this fashion suggests CIB1 may be redox regulated., Next to the bound GSH, the orientation of residues C35, H31, and S48 is, suggestive of a cysteine-type protein phosphatase active site. The, potential enzymatic activity of CIB1 is discussed and suggests a mechanism, by which it regulates a wide variety of proteins in cells in addition to, platelets.
+
<StructureSection load='1y1a' size='340' side='right'caption='[[1y1a]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==Disease==
+
<table><tr><td colspan='2'>[[1y1a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y1A FirstGlance]. <br>
-
Known disease associated with this structure: Multiple endocrine neoplasia, type IV OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600778 600778]]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-
 
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr>
-
==About this Structure==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y1a OCA], [https://pdbe.org/1y1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y1a RCSB], [https://www.ebi.ac.uk/pdbsum/1y1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y1a ProSAT]</span></td></tr>
-
1Y1A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=GSH:'>GSH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=CA1:Ca+Binding+Site+1,+Ef-Hand,+Chain+A'>CA1</scene>, <scene name='pdbsite=CA2:Ca+Binding+Site+2,+Ef-Hand,+Chain+A'>CA2</scene>, <scene name='pdbsite=CA3:Ca+Binding+Site+3,+Ef-Hand,+Chain+B'>CA3</scene> and <scene name='pdbsite=CA4:Ca+Binding+Site+4,+Ef-Hand,+Chain+B'>CA4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y1A OCA].
+
</table>
-
 
+
== Function ==
-
==Reference==
+
[https://www.uniprot.org/uniprot/CIB1_HUMAN CIB1_HUMAN] May convert the inactive conformation of integrin alpha-IIb/beta3 to an active form through binding to the integrin cytoplasmic domain. Induces cell migration and spreading mediated through integrin (possibly via focal adhesion complexes). Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. May play a role in regulation of apoptosis. Interacts with and up-regulates PTK2/FAK1 activity. Down regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Participates in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation.<ref>PMID:12714504</ref> <ref>PMID:12881299</ref> <ref>PMID:15685448</ref> <ref>PMID:18627437</ref> <ref>PMID:19805025</ref> <ref>PMID:21264284</ref>
-
The crystal structure of calcium- and integrin-binding protein 1: insights into redox regulated functions., Blamey CJ, Ceccarelli C, Naik UP, Bahnson BJ, Protein Sci. 2005 May;14(5):1214-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15840829 15840829]
+
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y1/1y1a_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1y1a ConSurf].
 +
<div style="clear:both"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Bahnson, B.J.]]
+
[[Category: Bahnson BJ]]
-
[[Category: Blamey, C.J.]]
+
[[Category: Blamey CJ]]
-
[[Category: Ceccarelli, C.]]
+
[[Category: Ceccarelli C]]
-
[[Category: Naik, U.P.]]
+
[[Category: Naik UP]]
-
[[Category: CA]]
+
-
[[Category: GSH]]
+
-
[[Category: calcium]]
+
-
[[Category: calcium-binding protein]]
+
-
[[Category: ef-hand]]
+
-
[[Category: glutathiolation]]
+
-
[[Category: glutathione]]
+
-
[[Category: integrin]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:22:23 2008''
+

Current revision

CRYSTAL STRUCTURE OF CALCIUM AND INTEGRIN BINDING PROTEIN

PDB ID 1y1a

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools