CAP-Gly domain: Difference between revisions

Line 5:

==Activity==

The cytoskeletal network contains Cytoskeleton-Associated Proteins (CAPs), including CLIP-170 and dynactins, that function in the organization of microtubules and in the transportation of vesicles and organelles. CAPs that bind to the +end of microtubules generally contain one or more glycine-rich domains with a well-conserved GKNDG sequence motif<ref>PMID:8480366</ref>, presumably involved in protein-protein binding.

The cytoskeletal network contains Cytoskeleton-Associated Proteins (CAPs), including CLIP-170 and dynactins, that function in the organization of microtubules and in the transportation of vesicles and organelles. CAPs that bind to the +end of microtubules generally contain one or more glycine-rich domains ("CAP-Gly" domains) with a well-conserved GKNDG sequence motif<ref>PMID:8480366</ref>, presumably involved in protein-protein binding.

==Structure==

The first crystal structure of a CAP-Gly domain (PDP file [[1lpl]]), from ~~Caenorhabditis~~ elegans protein F53F4.3, revealed a novel protein fold containing a small 5-strand antiparallel beta-barrel and an N-terminal helix. The GKNDG sequence is in two consecutive turns of a surface loop, at one side of a groove (as shown in image at left). The groove is lined by a large, concave patch of residues highly conserved among the related sequences<ref>PMID:12221106</ref>. In the crystal, a dimer is formed by binding of the C-terminus of each chain into the GKNDG groove of the other chain.

The first crystal structure of a CAP-Gly domain (PDP file [[1lpl]]), from C. elegans protein F53F4.3, revealed a novel protein fold containing a small 5-strand antiparallel beta-barrel, several loops, and an N-terminal helix. The GKNDG sequence is in two consecutive turns of a surface loop, at one side of a groove (as shown in image at left). The groove is lined by a large, concave patch of residues highly conserved among the related sequences<ref>PMID:12221106</ref>. In the crystal, a dimer is formed by binding of the C-terminus of each chain into the GKNDG groove of the other chain.

[[1tov|1TOV]] is a rebuilt and re-refined version of the same dataset from [[1lpl| 1LPL]], giving an improvement of about 4% in Rfree, identifying a sulfate (seen in both 2D and interactive images), and adding 3 more residues of ordered helix toward the N-terminal end of the domain fragment. Both are from the SouthEast Collaboratory for Structural Genomics (SECSG), solved by single wavelength sulfur-anomalous phasing. The new [[1tov]] structure was produced as part of a systematic 30-structure test of the then-new MolProbity methods for diagnosing and correcting problems in crystallographic models<ref>PMID:15965733</ref>.

[[1tov|1TOV]] is a rebuilt and re-refined version of the same dataset from [[1lpl| 1LPL]], giving an improvement of about 4% in Rfree, identifying a sulfate near the groove (seen in both 2D and interactive images), and adding 3 more residues of ordered helix toward the N-terminal end of the domain fragment. Both are from the SouthEast Collaboratory for Structural Genomics (SECSG), solved by single wavelength sulfur-anomalous phasing. The new [[1tov]] structure was produced as part of a systematic 30-structure test of the then-new MolProbity methods for diagnosing and correcting problems in crystallographic models<ref>PMID:15965733</ref>.

==References==

CAP-Gly domain: Difference between revisions

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@@ Line 5: / Line 5: @@
 ==Activity==
-The cytoskeletal network contains Cytoskeleton-Associated Proteins (CAPs), including CLIP-170 and dynactins, that function in the organization of microtubules and in the transportation of vesicles and organelles.  CAPs that bind to the +end of microtubules generally contain one or more glycine-rich domains with a well-conserved GKNDG sequence motif<ref>PMID:8480366</ref>, presumably involved in protein-protein binding.
+The cytoskeletal network contains Cytoskeleton-Associated Proteins (CAPs), including CLIP-170 and dynactins, that function in the organization of microtubules and in the transportation of vesicles and organelles.  CAPs that bind to the +end of microtubules generally contain one or more glycine-rich domains ("CAP-Gly" domains) with a well-conserved GKNDG sequence motif<ref>PMID:8480366</ref>, presumably involved in protein-protein binding.
 ==Structure==
-The first crystal structure of a CAP-Gly domain (PDP file [[1lpl]]), from Caenorhabditis elegans protein F53F4.3, revealed a novel protein fold containing a small 5-strand antiparallel beta-barrel and an N-terminal helix.  The GKNDG sequence is in two consecutive turns of a surface loop, at one side of a groove (as shown in image at left). The groove is lined by a large, concave patch of residues highly conserved among the related sequences<ref>PMID:12221106</ref>.  In the crystal, a dimer is formed by binding of the C-terminus of each chain into the GKNDG groove of the other chain.
+The first crystal structure of a CAP-Gly domain (PDP file [[1lpl]]), from C. elegans protein F53F4.3, revealed a novel protein fold containing a small 5-strand antiparallel beta-barrel, several loops, and an N-terminal helix.  The GKNDG sequence is in two consecutive turns of a surface loop, at one side of a groove (as shown in image at left). The groove is lined by a large, concave patch of residues highly conserved among the related sequences<ref>PMID:12221106</ref>.  In the crystal, a dimer is formed by binding of the C-terminus of each chain into the GKNDG groove of the other chain.
-[[1tov|1TOV]] is a rebuilt and re-refined version of the same dataset from [[1lpl| 1LPL]], giving an improvement of about 4% in Rfree, identifying a sulfate (seen in both 2D and interactive images), and adding 3 more residues of ordered helix toward the N-terminal end of the domain fragment.  Both are from the SouthEast Collaboratory for Structural Genomics (SECSG), solved by single wavelength sulfur-anomalous phasing.  The new [[1tov]] structure was produced as part of a systematic 30-structure test of the then-new MolProbity methods for diagnosing and correcting problems in crystallographic models<ref>PMID:15965733</ref>.
+[[1tov|1TOV]] is a rebuilt and re-refined version of the same dataset from [[1lpl| 1LPL]], giving an improvement of about 4% in Rfree, identifying a sulfate near the groove (seen in both 2D and interactive images), and adding 3 more residues of ordered helix toward the N-terminal end of the domain fragment.  Both are from the SouthEast Collaboratory for Structural Genomics (SECSG), solved by single wavelength sulfur-anomalous phasing.  The new [[1tov]] structure was produced as part of a systematic 30-structure test of the then-new MolProbity methods for diagnosing and correcting problems in crystallographic models<ref>PMID:15965733</ref>.
 ==References==
 <references/>