1s0p

<table><tr><td colspan='2'>[[1s0p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1pn1 1pn1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S0P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1S0P FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 ATCC 11735])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1s0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s0p OCA], [http://pdbe.org/1s0p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s0p RCSB], [http://www.ebi.ac.uk/pdbsum/1s0p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s0p ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CAP_DICDI CAP_DICDI]] May have a regulatory bifunctional role. Binds G-actin and PIP2. Involved in microfilament reorganization near the plasma membrane in a PIP2-regulated manner.

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== Publication Abstract from PubMed ==

Cyclase-associated proteins (CAPs) are widely distributed and highly conserved proteins that regulate actin remodeling in response to cellular signals. The N termini of CAPs play a role in Ras signaling and bind adenylyl cyclase; the C termini bind to G-actin and thereby alter the dynamic rearrangements of the microfilament system. We report here the X-ray structure of the core of the N-terminal domain of the CAP from Dictyostelium discoideum, which comprises residues 51-226, determined by a combination of single isomorphous replacement with anomalous scattering (SIRAS). The overall structure of this fragment is an alpha helix bundle composed of six antiparallel helices. Results from gel filtration and crosslinking experiments for CAP(1-226), CAP(255-464), and the full-length protein, together with the CAP N-terminal domain structure and the recently determined CAP C-terminal domain structure, provide evidence that the functional structure of CAP is multimeric.

Structure of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum.,Ksiazek D, Brandstetter H, Israel L, Bourenkov GP, Katchalova G, Janssen KP, Bartunik HD, Noegel AA, Schleicher M, Holak TA Structure. 2003 Sep;11(9):1171-8. PMID:12962635<ref>PMID:12962635</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Atcc 11735]]

[[Category: Bartunik, H D]]

[[Category: Bourenkov, G P]]

[[Category: Brandstetter, H]]

[[Category: Holak, T A]]

[[Category: Israel, L]]

[[Category: Janssen, K P]]

[[Category: Katchalova, G]]

[[Category: Ksiazek, D]]

[[Category: Noegel, A A]]

[[Category: Schleicher, M]]

[[Category: Membrane protein]]