Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

Songlin Li; Jim Finley; Zhi Jie Liu; Shi Hong Qiu; Hongli Chen; Chi Hao Luan; Mike Carson; Jun Tsao; David Johnson; Guangda Lin; Jun Zhao; Willie Thomas; Lisa A. Nagy; Bingdong Sha; Lawrence J. DeLucas; Bi Cheng Wang; Ming Luo

doi:10.1074/jbc.M208512200

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

Songlin Li, Jim Finley, Zhi Jie Liu, Shi Hong Qiu, Hongli Chen, Chi Hao Luan, Mike Carson, Jun Tsao, David Johnson, Guangda Lin, Jun Zhao, Willie Thomas, Lisa A. Nagy, Bingdong Sha, Lawrence J. DeLucas, Bi Cheng Wang, Ming Luo^*

^*Corresponding author for this work

CLP - High Throughput Analysis Lab

Research output: Contribution to journal › Article › peer-review

85 Scopus citations

Abstract

Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of the CAP-Gly domain of Caenorhabditis elegans F53F4.3 protein, solved by single wavelength sulfur-anomalous phasing, revealed a novel protein fold containing three β-sheets. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Residues in the groove are highly conserved as measured from the information content of the aligned sequences. The C-terminal tail of another molecule in the crystal is bound in this groove.

Original language	English (US)
Pages (from-to)	48596-48601
Number of pages	6
Journal	Journal of Biological Chemistry
Volume	277
Issue number	50
DOIs	https://doi.org/10.1074/jbc.M208512200
State	Published - Dec 13 2002

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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Li, S., Finley, J., Liu, Z. J., Qiu, S. H., Chen, H., Luan, C. H., Carson, M., Tsao, J., Johnson, D., Lin, G., Zhao, J., Thomas, W., Nagy, L. A., Sha, B., DeLucas, L. J., Wang, B. C., & Luo, M. (2002). Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain. Journal of Biological Chemistry, 277(50), 48596-48601. https://doi.org/10.1074/jbc.M208512200

@article{58ed432301c14e33ac01c96ec8b7be29,

title = "Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain",

abstract = "Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of the CAP-Gly domain of Caenorhabditis elegans F53F4.3 protein, solved by single wavelength sulfur-anomalous phasing, revealed a novel protein fold containing three β-sheets. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Residues in the groove are highly conserved as measured from the information content of the aligned sequences. The C-terminal tail of another molecule in the crystal is bound in this groove.",

author = "Songlin Li and Jim Finley and Liu, {Zhi Jie} and Qiu, {Shi Hong} and Hongli Chen and Luan, {Chi Hao} and Mike Carson and Jun Tsao and David Johnson and Guangda Lin and Jun Zhao and Willie Thomas and Nagy, {Lisa A.} and Bingdong Sha and DeLucas, {Lawrence J.} and Wang, {Bi Cheng} and Ming Luo",

year = "2002",

month = dec,

day = "13",

doi = "10.1074/jbc.M208512200",

language = "English (US)",

volume = "277",

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publisher = "American Society for Biochemistry and Molecular Biology Inc.",

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TY - JOUR

T1 - Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

AU - Li, Songlin

AU - Finley, Jim

AU - Liu, Zhi Jie

AU - Qiu, Shi Hong

AU - Chen, Hongli

AU - Luan, Chi Hao

AU - Carson, Mike

AU - Tsao, Jun

AU - Johnson, David

AU - Lin, Guangda

AU - Zhao, Jun

AU - Thomas, Willie

AU - Nagy, Lisa A.

AU - Sha, Bingdong

AU - DeLucas, Lawrence J.

AU - Wang, Bi Cheng

AU - Luo, Ming

PY - 2002/12/13

Y1 - 2002/12/13

N2 - Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of the CAP-Gly domain of Caenorhabditis elegans F53F4.3 protein, solved by single wavelength sulfur-anomalous phasing, revealed a novel protein fold containing three β-sheets. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Residues in the groove are highly conserved as measured from the information content of the aligned sequences. The C-terminal tail of another molecule in the crystal is bound in this groove.

AB - Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of the CAP-Gly domain of Caenorhabditis elegans F53F4.3 protein, solved by single wavelength sulfur-anomalous phasing, revealed a novel protein fold containing three β-sheets. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Residues in the groove are highly conserved as measured from the information content of the aligned sequences. The C-terminal tail of another molecule in the crystal is bound in this groove.

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U2 - 10.1074/jbc.M208512200

DO - 10.1074/jbc.M208512200

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SN - 0021-9258

VL - 277

SP - 48596

EP - 48601

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 50

ER -

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

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